Plastics have quickly become an integral part of modern life. Due to excessive production and improper waste disposal, they are recognized as contaminants present in practically all habitat types. Although there are several polymers, polyethylene terephthalate (PET) is of particular concern due to its abundance in the environment. There is a need for a solution that is both cost-effective and ecologically friendly to address this pollutant. The use of microbial depolymerizing enzymes could offer a biological avenue for plastic degradation, though the full potential of these enzymes is yet to be uncovered. The purpose of this study was to use (1) plate-based screening methods to investigate the plastic degradation potential of marine bacteria from the order Enterobacterales collected from various organismal and environmental sources, and (2) perform genome-based analysis to identify polyesterases potentially related to PET degradation. 126 bacterial isolates were obtained from the strain collection of RD3, Research Unit Marine Symbioses-GEOMAR-and sequentially tested for esterase and polyesterase activity, in combination here referred to as PETase–like activity. The results show that members of the microbial families Alteromonadaceae, Shewanellaceae, and Vibrionaceae, derived from marine sponges and bryozoans, are the most promising candidates within the order Enterobacterales. Furthermore, 389 putative hydrolases from the α/β superfamily were identified in 23 analyzed genomes, of which 22 were sequenced for this study. Several candidates showed similarities with known PETases, indicating underlying enzymatic potential within the order Enterobacterales for PET degradation.
Citation: Denisse Galarza–Verkovitch, Onur Turak, Jutta Wiese, Tanja Rahn, Ute Hentschel, Erik Borchert. Bioprospecting for polyesterase activity relevant for PET degradation in marine Enterobacterales isolates[J]. AIMS Microbiology, 2023, 9(3): 518-539. doi: 10.3934/microbiol.2023027
[1] | Yangtao Wang, Kelin Li . Exponential synchronization of fractional order fuzzy memristor neural networks with time-varying delays and impulses. Mathematical Modelling and Control, 2025, 5(2): 164-179. doi: 10.3934/mmc.2025012 |
[2] | Anil Chavada, Nimisha Pathak, Sagar R. Khirsariya . A fractional mathematical model for assessing cancer risk due to smoking habits. Mathematical Modelling and Control, 2024, 4(3): 246-259. doi: 10.3934/mmc.2024020 |
[3] | Ihtisham Ul Haq, Nigar Ali, Hijaz Ahmad . Analysis of a chaotic system using fractal-fractional derivatives with exponential decay type kernels. Mathematical Modelling and Control, 2022, 2(4): 185-199. doi: 10.3934/mmc.2022019 |
[4] | Abduljawad Anwar, Shayma Adil Murad . On the Ulam stability and existence of Lp-solutions for fractional differential and integro-differential equations with Caputo-Hadamard derivative. Mathematical Modelling and Control, 2024, 4(4): 439-458. doi: 10.3934/mmc.2024035 |
[5] | Iman Malmir . Novel closed-loop controllers for fractional nonlinear quadratic systems. Mathematical Modelling and Control, 2023, 3(4): 345-354. doi: 10.3934/mmc.2023028 |
[6] | Mrutyunjaya Sahoo, Dhabaleswar Mohapatra, S. Chakraverty . Wave solution for time fractional geophysical KdV equation in uncertain environment. Mathematical Modelling and Control, 2025, 5(1): 61-72. doi: 10.3934/mmc.2025005 |
[7] | Lusong Ding, Weiwei Sun . Neuro-adaptive finite-time control of fractional-order nonlinear systems with multiple objective constraints. Mathematical Modelling and Control, 2023, 3(4): 355-369. doi: 10.3934/mmc.2023029 |
[8] | C. Kavitha, A. Gowrisankar . Fractional integral approach on nonlinear fractal function and its application. Mathematical Modelling and Control, 2024, 4(3): 230-245. doi: 10.3934/mmc.2024019 |
[9] | Kexin Ouyang, Xinmin Qu, Huiqin Lu . Sign-changing and signed solutions for fractional Laplacian equations with critical or supercritical nonlinearity. Mathematical Modelling and Control, 2025, 5(1): 1-14. doi: 10.3934/mmc.2025001 |
[10] | Muhammad Nawaz Khan, Imtiaz Ahmad, Mehnaz Shakeel, Rashid Jan . Fractional calculus analysis: investigating Drinfeld-Sokolov-Wilson system and Harry Dym equations via meshless procedures. Mathematical Modelling and Control, 2024, 4(1): 86-100. doi: 10.3934/mmc.2024008 |
Plastics have quickly become an integral part of modern life. Due to excessive production and improper waste disposal, they are recognized as contaminants present in practically all habitat types. Although there are several polymers, polyethylene terephthalate (PET) is of particular concern due to its abundance in the environment. There is a need for a solution that is both cost-effective and ecologically friendly to address this pollutant. The use of microbial depolymerizing enzymes could offer a biological avenue for plastic degradation, though the full potential of these enzymes is yet to be uncovered. The purpose of this study was to use (1) plate-based screening methods to investigate the plastic degradation potential of marine bacteria from the order Enterobacterales collected from various organismal and environmental sources, and (2) perform genome-based analysis to identify polyesterases potentially related to PET degradation. 126 bacterial isolates were obtained from the strain collection of RD3, Research Unit Marine Symbioses-GEOMAR-and sequentially tested for esterase and polyesterase activity, in combination here referred to as PETase–like activity. The results show that members of the microbial families Alteromonadaceae, Shewanellaceae, and Vibrionaceae, derived from marine sponges and bryozoans, are the most promising candidates within the order Enterobacterales. Furthermore, 389 putative hydrolases from the α/β superfamily were identified in 23 analyzed genomes, of which 22 were sequenced for this study. Several candidates showed similarities with known PETases, indicating underlying enzymatic potential within the order Enterobacterales for PET degradation.
The notion of metric geometric mean (MGM for short) of positive definite matrices involves many mathematical areas, e.g. matrix/operator theory, geometry, and group theory. For any positive definite matrices A and B of the same size, the MGM of A and B is defined as
A♯B=A1/2(A−1/2BA−1/2)1/2A1/2. | (1.1) |
From algebraic viewpoint, A♯B is a unique positive solution of the Riccati equation (see [1, Ch. 4])
XA−1X=B. | (1.2) |
In fact, the explicit formula (1.1) and the equation (1.2) are two equivalent ways to describe the geometric mean; see [2]. From differential-geometry viewpoint, A♯B is a unique midpoint of the Riemannian geodesic interpolated from A to B, called the weighted geometric mean of A and B:
γ(t):=A♯tB=A1/2(A−1/2BA−1/2)tA1/2,0⩽t⩽1. | (1.3) |
This midpoint is measured through a natural Riemannian metric; see a monograph [1, Ch. 6] or Section 2. The weighted MGMs (1.3) posses rich algebraic, order, and analytic properties, namely, positive homogeneity, congruent invariance, permutation invariance, self duality, monotonicity, and continuity from above; see [3, Sect. 3].
In operator-theoretic approach, the weighted MGMs (1.3) for positive operators on a Hilbert space are Kubo-Ando means [4] in the sense that they satisfy the monotonicity, transformer inequality, continuity from above, and normalization. More precisely, A♯tB is the Kubo-Ando mean associated with the operator monotone function f(x)=xt on the positive half-line, e.g. [3, Sect. 3]. The geometric mean serves as a tool for deriving matrix/operators inequalities; see the original idea in [5], see also [1, Ch. 4], [3, Sect. 3], and [6]. The cancellability of the weighted MGM together with spectral theory can be applied to solve operator mean equations; see [7]. Indeed, given two positive invertible operators A and B acting on the same Hilbert space (or positive definite matrices of the same dimension), the equation A♯tX=B is uniquely solvable in terms of the weighted MGM in which the weight can be any nonzero real number. See more development of geometric mean theory for matrices/operators in [8,9,10].
A series of Lawson and Lim works investigated the theory of (weighted) MGM in various frameworks. Indeed, the geometric mean (with weight 1/2) can be naturally defined on symmetric cones [11], symmetric sets [12], two-powered twisted subgroups [12,13], and Bruhat-Tits spaces [2]. The framework of reflection quasigroups (based on point-reflection geometry and quasigroup theory) [13] allows us to define weighted MGMs via geodesics, where the weights can be any dyadic rationals. On lineated symmetric spaces [14], the weights can be arbitrary real numbers, due to the density of the dyadic rationals on the real line. Their theory can be applied to solve certain symmetric word equations in two matrix letters; see [15]. Moreover, mean equations related MGMs were investigated in [13,16].
From the formulas (1.1) and (1.3), the matrix products are the usual products between matching-dimension matrices. We can extend the MGM theory by replacing the usual product to the semi-tensor product (STP) between square matrices of general dimension. The STP was introduced by Cheng [17], so that the STP reduces to the usual matrix product in matching-dimension case. The STP keeps various algebraic properties of the usual matrix product such as the distribution over the addition, the associativity, and compatibility with transposition, inversion and scalar multiplication. The STP is a useful tool when dealing with vectors and matrices in classical and fuzzy logic, lattices and universal algebra, and differential geometry; see [18,19]. The STPs turn out to have a variety of applications in other fields: networked evolutionary games [20], finite state machines [21], Boolean networks [19,22,23], physics [24], and engineering [25]. Many authors developed matrix equations based on STPs; e.g. Sylvester-type equations [26,27,28], and a quadratic equation A⋉X⋉X=B [29].
The present paper aims to develop further theory on weighted MGMs for positive definite matrices of arbitrary dimensions, where the matrix products are given by the STPs. In this case, the weights can be arbitrary real numbers; see Section 3. It turns out that this mean satisfies various properties as in the classical case. The most interesting case is when the weights belong to the unit interval. In this case, the weighted MGM satisfies the monotonicity, and the continuity from above. Then we investigate the theory when either A or B is not assumed to be invertible. In such case, the weights are restricted to be in [0,∞) or (−∞,1]. We also use a continuity argument to study the weighted MGMs, in which the weights belong to [0,1]. Moreover, we prove the cancellability of the weighted MGMs, and apply to solve certain nonlinear matrix equations concerning MGMs; see Section 4. In Section 5, we apply the theory to solve the Riccati equation and certain symmetric word equations in two matrix letters. Finally, we summarize the whole work in Section 6.
In the next section, we setup basic notation and provide preliminaries results on the Riemannian geometry of positive definite matrices, the tensor product, and the semi-tensor product.
Throughout, let Mm,n be the set of all m×n complex matrices, and abbreviate Mn,n to Mn. Define Cn=Mn,1, the set of n-dimensional complex vectors. Denote by AT and A∗ the transpose and conjugate transpose of a matrix A, respectively. The n×n identity matrix is denoted by In. The general linear group of n×n invertible complex matrices is denoted by GLn. The symbols Hn, and PSn stand for the vector space of n×n Hermitian matrices, and the cone of n×n positive semidefinite matrices, respectively. For a pair (A,B)∈Hn×Hn, the partial ordering A⩾B means that A−B lies in the positive cone PSn. In particular, A∈PSn if and only if A⩾0. Let us denote the set of n×n positive definite matrices by Pn. For each A∈Hn, the strict inequality A>0 indicates that A∈Pn.
A matrix pair (A,B)∈Mm,n×Mp,q is said to satisfy factor-dimension condition if n|p or p|n. In this case, we write A≻kB when n=kp, and A≺kB when p=kn.
Recall that Mn is a Hilbert space endowed with the Hilbert-Schmidt inner product ⟨A,B⟩HS=trA∗B and the associated norm ‖A‖HS=(trA∗A)1/2. The subset Pn, which is an open subset in Hn, is a Riemannian manifold endowed with the trace Riemannian
ds=‖A−1/2dAA−1/2‖HS=[tr(A−1dA)2]1/2. |
If γ:[a,b]→Pn is a (piecewise) differentiable path in Pn, we define the length of γ by
L(γ)=∫ba‖γ−1/2(t)γ′(t)γ−1/2(t)‖HSdt. |
For each X∈GLn, the congruence transformation
ΓX:Pn→Pn,A↦X∗AX | (2.1) |
is bijective and the composition ΓX∘γ:[a,b]→Pn is another path in Pn. For any A,B∈Pn, the distance between A and B is given by
δHS(A,B)=inf{ L(γ):γ is a path from A to B }. |
Lemma 2.1. (e.g. [1]). For each A,B∈Pn, there is a unique geodesic from A to B, parametrized by
γ(t)=A1/2(A−1/2BA−1/2)tA1/2,0⩽t⩽1. | (2.2) |
This geodesic is natural in the sense that δHS(A,γ(t))=tδHS(A,B) for each t.
For any A,B∈Pn, denote the geodesic from A to B by [A,B].
This subsection is a brief review on tensor products and semi-tensor products of matrices. Recall that for any matrices A=[aij]∈Mm,n and B∈Mp,q, their tensor product is defined by
A⊗B=[aijB]∈Mmp,nq. |
The tensor operation (A,B)↦A⊗B is bilinear and associative.
Lemma 2.2 (e.g. [3]). Let (A,B)∈Mm,n×Mp,q and (P,Q)∈Mm×Mn. Then we have
(1). A⊗B=0 if and only if either A=0 or B=0;
(2). (A⊗B)∗=A∗⊗B∗;
(3). if (P,Q)∈GLm×GLn, then (P⊗Q)−1=P−1⊗Q−1;
(4). if (P,Q)∈PSm×PSn, then P⊗Q∈PSmn and (P⊗Q)1/2=P1/2⊗Q1/2;
(5). if (P,Q)∈Pm×Pn, then P⊗Q∈Pmn;
(6). det(P⊗Q)=(detP)n(detQ)m.
To define the semi-tensor product, first consider a pair (X,Y)∈M1,m×Cn of row and column vectors, respectively. If X≻kY, then we split X into X1,X2,…,Xn∈M1,k and define the STP of X and Y as
X⋉Y=n∑i=1yiXi∈M1,k. |
If X≺kY, then we split Y into Y1,Y2,…,Ym∈Ck and define the STP of X and Y as
X⋉Y=m∑i=1xiYi∈Ck. |
In general, for a pair (A,B)∈Mm,n×Mp,q satisfying the factor-dimensional condition, we define
A⋉B=[Ai⋉Bj]m,qi,j=1, |
where Ai is i-th row of A and Bj is the j-th column of B. More generally, for an arbitrary matrix pair (A,B)∈Mm,n×Mp,q, we let α=lcm(n,p) and define
A⋉B=(A⊗Iα/n)(B⊗Iα/p)∈Mαmn,αqp. |
The operation (A,B)↦A⋉B turns out to be bilinear, associative, and continuous.
Lemma 2.3 (e.g. [18]). Let (A,B)∈Mm,n×Mp,q and (P,Q)∈Mm×Mn. Then we have
(1). (A⋉B)∗=B∗⋉A∗;
(2). if (P,Q)∈GLm×GLn, then (P⋉Q)−1=Q−1⋉P−1;
(3). det(P⋉Q)=(detP)α/m(detQ)α/n where α=lcm(m,n).
Proposition 2.4. Let A∈Mm,X∈Mn and S,T∈Hm.
(1). If A⩾0, then X∗⋉A⋉X⩾0.
(2). If S⩾T, then X∗⋉S⋉X⩾X∗⋉T⋉X.
(3). If A>0 and X∈GLn, then X∗⋉A⋉X>0.
(4). If S>T, then X∗⋉S⋉X>X∗⋉T⋉X.
Proof. 1) Since (X∗⋉A⋉X)∗=X∗⋉A⋉X, we have that X∗⋉A⋉X is Hermitian. Let α=lcm(m,n) and u∈Cα. Set v=X⋉u. Using Lemma 2.2, we obtain that A⊗Iα/p⩾0 and then, by Lemma 2.3,
u∗(X∗⋉A⋉X)u=(X⋉u)∗⋉A⋉(X⋉u)=v∗(A⊗Iα/n)v⩾0. |
This implies that X∗⋉A⋉X⩾0. 2) Since S⩾T, we have S−T⩾0. Applying the assertion 1, we get X∗⋉(S−T)⋉X⩾0, i.e., X∗⋉S⋉X⩾X∗⋉T⋉X. The proofs of the assertions 3)-4) are similar to the assertions 1)-2), respectively.
We extend the classical weighted MGM (1.3) for a pair of positive definite matrices of different sizes as follows.
Definition 3.1. Let (A,B)∈Pm×Pn. For any t∈R, the t-weighted metric geometric mean (MGM) of A and B is defined by
A♯tB=A1/2⋉(A−1/2⋉B⋉A−1/2)t⋉A1/2∈Mα, | (3.1) |
where α=lcm(m,n).
Note that when m=n, Eq (3.1) reduces to the classical one (1.3). In particular, A♯0B=A⊗Iα/m, A♯1B=B⊗Iα/n, A♯−1B=A⋉B−1⋉A, and A♯2B=B⋉A−1⋉B. Fundamental properties of the weighted MGMs (3.1) are as follows.
Theorem 3.2. Let (A,B)∈Pm×Pn. Let r,s,t∈R and α=lcm(m,n). Then
(1). Positivity: A♯tB>0.
(2). Fixed-point property: A♯tA=A.
(3). Positive homogeneity: c(A♯tB)=(cA)♯t(cB) for all c>0.
(4). Congruent invariance: C∗(A♯tB)C=(C∗⋉A⋉C)♯t(C∗⋉B⋉C) for all C∈GLα.
(5). Self duality: (A♯tB)−1=A−1♯tB−1.
(6). Permutation invariance: A♯1/2B=B♯1/2A. More generally, A♯tB=B♯1−tA.
(7). Affine change of parameters: (A♯rB)♯t(A♯sB)=A♯(1−t)r+tsB.
(8). Exponential law: A♯r(A♯sB)=A♯rsB.
(9). C♯−1(A♯tB)=(C♯−1A)♯t(C♯−1B) for any C∈Pm.
(10). Left cancellability: Let Y1,Y2∈Pn and t∈R−{0}. Then the equation A♯tY1=A♯tY2 implies Y1=Y2. In other words, for each t≠0, the map X↦A♯tX is an injective map from Pn to Pα.
(11). Right cancellability: Let X1,X2∈Pm and t∈R−{1}. Then the equation X1♯tB=X2♯tB implies X1=X2. In other words, for each t≠1, the map X↦X♯tB is an injective map from Pm to Pα.
(12). Determinantal identity: det(A♯tB)=(detA)(1−t)αm(detB)tαn.
Proof. The positivity of ♯t follows from Proposition 2.4(3). Properties 2 and 3 follow directly from the formula (3.1). Let γ be the natural parametrization of the geodesic [A⊗Iα/m,B⊗Iα/n] on the space Pα as discussed in Lemma 2.1. To prove the congruent invariance, let C∈GLα and consider the congruence transformation ΓC defined by (2.1). Then the path γC(t):=ΓC(γ(t)) joins the points γC(0)=C∗⋉A⋉C and γC(1)=C∗⋉B⋉C. By Lemma 2.1, we obtain
C∗(A♯tB)C=ΓC(γ(t))=γC(t)=(C∗⋉A⋉C)♯t(C∗⋉B⋉C). |
To prove the self duality, let β(t)=(γ(t))−1. By Lemma 2.2, we have β(0)=A−1⊗Iα/m and β(1)=B−1⊗Iα/n. Thus
(A♯tB)−1=(γ(t))−1=β(t)=A−1♯tB−1. |
To prove the 6th item, define f:R→R by f(t)=1−t. Let δ=γ∘f. Then δ(0)=B⊗Iα/n and δ(1)=A⊗Iα/m. By Lemma 2.1, we have δ(t)=B♯tA, and thus
A♯tB=γ(t)=γ(f(1−t))=δ(1−t)=B♯1−tA. |
To prove the 7th item, fix r,s and let t vary. Let δ(t)=(A♯rB)♯t(A♯sB). We have δ(0)=A♯rB and δ(1)=A♯sB. Define f:R→R,f(t)=(1−t)r+ts and β=γ∘f. We obtain
β(t)=γ((1−t)r+ts)=A♯(1−t)r+tsB |
and β(0)=A♯rB, β(1)=A♯sB. Hence, δ(t)=β(t), i.e., (A♯rB)♯t(A♯sB)=A♯(1−t)r+tsB. The exponential law is derived from the 7th item as follows: A♯r(A♯sB)=(A♯0B)♯r(A♯sB)=A♯rsB. The 9th item follows from the congruent invariance and the self duality. To prove the left cancellability, let t∈R−{0} and suppose that A♯tY1=A♯tY2. We have by the exponential law that
Y1⊗Iα/n=A♯1Y1=A♯1/t(A♯tY1)=A♯1/t(A♯tY2)=A♯1Y2=Y2⊗Iα/n. |
It follows that (Y1−Y2)⊗Iα/n=0, and thus by Lemma 2.2 we conclude that Y1=Y2. Hence, the map X↦A♯tX is injective. The right cancellability follows from the left cancellability together with the permutation inavariance. The determinantal identity follows directly from Lemmas 2.3 and 2.2:
det(A♯tB)=det(A1/2)α/mdet((A−1/2⋉B⋉A−1/2)t)(detA1/2)α/m=(detA)α/m(det(A−1/2⋉B⋉A−1/2)t)=(detA)α/m(detA)−tα/m(detB)tα/n=(detA)(1−t)α/m(detB)tα/n. |
This finishes the proof.
Remark 3.3. From Theorem 3.2, a particular case of the exponential law is that (Bs)r=Bsr for any B>0 and s,t∈R. The congruent invariance means that the operation ♯t is invariant under the congruence transformation ΓC for any C∈GLα.
Now, we focus on weighted MGMs in which the weight lies in the interval [0,1]. Let us write Ak→A when the matrix sequence (Ak) converges to the matrix A. If (Ak) is a sequence in Hn, the expression Ak↓A means that (Ak) is a decreasing sequence and Ak→A. Recall the following well known matrix inequality:
Lemma 3.4 (Löwner-Heinz inequality, e.g. [3]). Let S,T∈PSn and w∈[0,1]. If S⩽T, then Sw⩽Tw.
When the weights are in [0,1], this mean has remarkable order and analytic properties:
Theorem 3.5. Let (A,B),(C,D)∈Pm×Pn and w∈[0,1].
(1). Monotonicity: If A⩽C and B⩽D, then A♯wB⩽C♯wD.
(2). Continuity from above: Let (Ak,Bk)∈Pm×Pn for all k∈N. If Ak↓A and Bk↓B, then Ak♯wBk↓A♯wB.
Proof. To prove the monotonicity, suppose that A⩽C and B⩽D. By Proposition 2.4, we have that A−1/2⋉B⋉A−1/2⩽A−1/2⋉D⋉A−1/2. Using Lemma 3.4 and Proposition 2.4, we obtain
A♯wB=A1/2⋉(A−1/2⋉B⋉A−1/2)w⋉A1/2⩽A1/2⋉(A−1/2⋉D⋉A−1/2)w⋉A1/2=A♯wD. |
This shows the monotonicity of ♯w in the second argument. This property together with the permutation invariance in Theorem 3.2 yield
A♯wB=B♯1−wA⩽B♯1−wC=C♯wB⩽C♯wD. |
To prove the continuity from above, suppose that Ak↓A and Bk↓B. Applying the monotonicity and the positivity, we conclude that (Ak♯wBk) is a decreasing sequence of positive definite matrices. The continuity of the semi-tensor multiplication implies that A−1/2k⋉Bk⋉A−1/2k converges to A−1/2⋉B⋉A−1/2, and thus
A1/2k⋉(A−1/2k⋉Bk⋉A−1/2k)w⋉A1/2k→A1/2⋉(A−1/2⋉B⋉A−1/2)w⋉A1/2. |
Hence, Ak♯wBk↓A♯wB.
Now, we extend the weighted MGM to positive semidefinite matrices. Indeed, when the first matrix argument is positive definite but the second one is positive semidefinite, the weights can be any nonnegative real numbers.
Definition 3.6. Let (A,B)∈Pm×PSn. For any t∈[0,∞), the t-weighted MGM of A and B is defined by
A♯tB=A1/2⋉(A−1/2⋉B⋉A−1/2)t⋉A1/2. | (3.2) |
Here, we apply a convention X0=Iα for any X∈Mα.
This definition is well-defined since the matrix A−1/2⋉B⋉A−1/2 is positive semidefinite according to Proposition 2.4. The permutation invariance suggests the following definition.
Definition 3.7. Let (A,B)∈PSm×Pn. For any t∈(−∞,1], the t-weighted MGM of A and B is defined by
A♯tB=B♯1−tA=B1/2⋉(B−1/2⋉A⋉B−1/2)1−t⋉B1/2. | (3.3) |
Here, we apply the convention X0=Iα for any X∈Mα.
This definition is well-defined according to Definition 3.6 (since 1−t⩾0). Note that when A>0 and B>0, Definitions 3.1, 3.6, and 3.7 are coincide. Fundamental properties of the means (3.2) and (3.3) are as follows.
Theorem 3.8. Denote α=lcm(m,n). If either
(i) (A,B)∈Pm×PSn and r,s,t⩾0, or
(ii) (A,B)∈PSm×Pn and r,s,t⩽1,
then
(1). Positivity: A♯tB⩾0.
(2). Positive homogeneity: c(A♯tB)=(cA)♯t(cB) for all c>0.
(3). Congruent invariance: C∗(A♯tB)C=(C∗⋉A⋉C)♯t(C∗⋉B⋉C) for all C∈GLα.
(4). Affine change of parameters: (A♯rB)♯t(A♯sB)=A♯(1−t)r+tsB.
(5). Exponential law: A♯r(A♯sB)=A♯rsB.
(6). Determinantal identity: det(A♯tB)=(detA)(1−t)αm(detB)tαn.
Proof. The proof of each assertion is similar to that in Theorem 3.2. When A∈PSm, we consider A+ϵIm∈Pm and take limits when ϵ→0+. When B∈PSn, we consider B+ϵIn∈Pn and take limits when ϵ→0+.
It is natural to extend the weighted MGMs of positive definite matrices to those of positive semidefinite matrices by a limit process. Theorem 3.5 (or both Definitions 3.6 and 3.7) then suggests us that the weights must be in the interval [0,1].
Definition 3.9. Let (A,B)∈PSm×PSn. For any w∈[0,1], the w-weighted MGM of A and B is defined by
A♯wB=limε↓0+(A+εIm)♯w(B+εIn)∈Mα, | (3.4) |
where α=lcm(m,n). Here, we apply the convention X0=Iα for any X∈Mα.
Lemma 3.10. Definition 3.4 is well-defined. Moreover, if (A,B)∈PSm×PSn, then A♯wB∈PSα.
Proof. When ε↓0+, the nets A+εIm and B+εIn are decreasing nets of positive definite matrices. From the monotonicity property in Theorem 3.5, the net (A+εIm)♯w(B+εIn) is decreasing. Since this net is also bounded below by the zero matrix, the order-completeness of the matrix space guarantees an existence of the limit (3.4). Moreover, the matrix limit is positive semidefinite.
Fundamental properties of weighted MGMs are listed below.
Theorem 3.11. Let (A,B),(C,D)∈PSm×PSn. Let w,r,s∈[0,1] and α=lcm(m,n). Then
(1). Fixed-point property: A♯wA=A.
(2). Positive homogeneity: c(A♯wB)=(cA)♯w(cB) for all c⩾0.
(3). Congruent invariance: T∗⋉(A♯wB)⋉T=(T∗⋉A⋉T)♯w(T∗⋉B⋉T) for all T∈GLα.
(4). Permutation invariance: A♯1/2B=B♯1/2A. More generally, A♯wB=B♯1−wA.
(5). Affine change of parameters: (A♯rB)♯w(A♯sB)=A♯(1−w)r+wsB.
(6). Exponential law: A♯r(A♯sB)=A♯rsB.
(7). Determinantal identity: det(A♯wB)=(detA)(1−w)αm(detB)wαn.
(8). Monotonicity: If A⩽C and B⩽D, then A♯wB⩽C♯wD.
(9). Continuity from above: If Ak∈PSm and Bk∈PSn for all k∈N are such that Ak↓A and Bk↓B, then Ak♯wBk↓A♯wB.
Proof. When A∈PSm and B∈PSn, we can consider A+εIm∈Pm and B+εIn∈Pn, and then take limits when ε→0+. The 1st-7th items now follow from Theorem 3.2 (or Theorems 3.8). The 8th-9th items follow from Theorem 3.5. For the continuity from above, if Ak↓A and Bk↓B, then the monotonicity implies the decreasingness of the sequence Ak♯wBk when k→∞. Moreover,
limk→∞Ak♯wBk=limk→∞limε→0+(Ak+εIm)♯w(Bk+εIn)=limε→0+limk→∞(Ak+εIm)♯w(Bk+εIn)=limε→0+(A+εIm)♯w(B+εIn)=A♯wB. |
Thus, Ak♯wBk↓A♯wB as desire.
In particular, the congruent invariance implies the transformer inequality:
C⋉(A♯wB)⋉C⩽(C⋉A⋉C)♯w(C⋉B⋉C),C⩾0. |
This property together with the monotonicity, the above continuity, and the fixed-point property yield that the mean ♯w is a Kubo-Ando mean when w∈[0,1]. The results in this section include those for the MGM with weight 1/2 in [30].
In this section, we apply our theory to solve certain matrix equations concerning weighted MGMs for positive definite matrices.
Corollary 4.1. Let A∈Pm and B,X∈Pn with A≺kB. Let t∈R−{0}. Then the mean equation
A♯tX=B | (4.1) |
is uniquely solvable with an explicit solution X=A♯1/tB. Moreover, the solution varies continuously on the given matrices A and B. In particular, the geometric mean problem A♯1/2X=B has a unique solution X=A♯2B=B⋉A−1⋉B.
Proof. The exponential law in Theorem 3.2 implies that
A♯tX=B=A♯1B=A♯t(A♯1/tB). |
Then the left cancellability implies that Eq (4.1) has a unique solution X=A♯1/tB. The continuity of the solution follows from the explicit formula (3.1) and the continuity of the semi-tensor operation.
Remark 4.2. We can investigate the Eq (4.1) when A∈Pm and B∈PSn. In this case, the weight t must be positive. This equation is uniquely solvable with an explicit solution X=A♯1/tB∈PSn. For simplicity in this section, we consider only the case when all given matrices are positive definite.
Corollary 4.3. Let A∈Pm and B,X∈Pn with A≺kB. Let r,s,t∈R.
(1). If s≠0 and t≠1, then the mean equation
(A♯sX)♯tA=B | (4.2) |
is uniquely solvable with an explicit solution X=A♯1s(1−t)B.
(2). If s+t≠st, then the equation
(A♯sX)♯tX=B | (4.3) |
is uniquely solvable with an explicit solution X=A♯λB, where λ=1/(s+t−st).
(3). If s(1−t)≠1, then the mean equation
(A♯sX)♯tB=X | (4.4) |
is uniquely solvable with an explicit solution X=A♯λB, where λ=t/(st−s+1).
(4). If s≠t, then the equation
A♯sX=B♯tX | (4.5) |
is uniquely solvable with an explicit solution X=A♯λB, where λ=(1−t)/(s−t).
(5). If s−rs+rt≠1, then the equation
(A♯sX)♯r(B♯tX)=X | (4.6) |
is uniquely solvable with an explicit solution X=A♯λB, where λ=(rt−r)/(s−rs+rt−1).
(6). If t≠0, then the mean equation
(A♯tX)♯r(B♯tX)=X | (4.7) |
is uniquely solvable with an explicit solution X=A♯rB.
Proof. For the 1st assertion, using Theorem 3.2, we have
A♯s(1−t)X=A♯1−t(A♯sX)=(A♯sX)♯tA=B. |
By Corollary 4.1, we get the desire solution.
For the 2nd item, applying Theorem 3.2, we get
A♯s+t−stX=X♯(1−s)(1−t)A=X♯1−t(X♯1−sA)=(A♯sX)♯tX=B. |
Using Corollary 4.1, we obtain that X=A♯1s+t−stB.
For the 3rd item, the trivial case s=t=0 yields X=A♯0B. Assume that s,t≠0. From B♯1−t(A♯sX)=X, we get by Theorem 3.2 and Corollary 4.1 that A♯sX=B♯11−tX=X♯tt−1B. Consider
B=X♯t−1t(A♯sX)=X♯t−1t(X♯1−sA)=X♯(t−1)(1−s)tA=A♯1λX, |
where λ=t/(st−s+1). Now, we can deduce the desire solution from Corollary 4.1.
For the 4th item, the trivial case s=0 yields that the equation B♯tX=A⊗Ik has a unique solution X=B♯1tA=A♯t−1tB. Now, consider the case s≠0. Using Corollary 4.1, we have
X=A♯1s(B♯tX)=(B♯tX)♯s−1sA. |
Applying (4.4), we obtain that X=B♯(s−1)/(s−t)A=A♯λB, where λ=(1−t)/(s−t).
For the 5th item, the case r=0 yields that the equation A♯sX=X has a unique solution X=A♯0B. Now, consider the case r≠0. Using Theorem 3.2 and Corollary 4.1, we get
B♯tX=(A♯sX)♯1rX=X♯r−1r(X♯1−sA)=X♯(r−1)(1−s)rA=A♯rs−s+1rX. |
Applying the equation (4.5), we obtain that X=A♯λB, where λ=rt/(s−rs+rt).
For the 6th item, setting s=t in (4.6) yields the desire result.
Remark 4.4. Note that the cases t=0 in Eqs (4.1)–(4.5) all reduce to Eq (4.1). A particular case of (4.3) when s=t=1/2 reads that the mean equation
(A♯X)♯X=B | (4.8) |
has a unique solution X=A♯4/3B. In Eq (4.4), when s=t=1/2, the mean equation
(A♯X)♯B=X |
has a unique solution X=A♯2/3B. If r=s=t=1/2, then Eqs (4.6) or (4.7) implies that the geometric mean X=A♯B is a unique solution of the equation
(A♯X)♯(B♯X)=X. | (4.9) |
Equtions (4.8) and (4.9) were studied in [13] in the framework of dyadic symmetric sets.
Recall that a matrix word in two letters A,B∈Mn is an expression of the form
W(A,B)=Ar1Bs1Ar2Bs2⋯ArpBspArp+1 |
in which the exponents ri,si∈R−{0} for all i=1,2,…,p and rp+1∈R. A matrix word is said to be symmetric if it is identical to its reversal. A famous symmetric matrix-word equation is the Riccati equation
XAX=B, | (5.1) |
here A,B,X are positive definite matrices of the same dimension. Indeed, in control engineering, an optimal regulator problem for a linear dynamical system reduces to an algebraic Riccati equation (under the controllability and the observability conditions) X∗A−1X−R∗X−X∗R=B, where A,B are positive definite, and R is an arbitrary square matrix. A simple case R=0 yields the Riccati equation X∗A−1X=B.
In our context, the Riccati equation (5.1) can be written as A−1♯2X=B or X♯−1A−1=B. The case t=2 in Corollary 4.1 reads:
Corollary 5.1. Let A∈Pm and B,X∈Pn with A≺kB. Then the Riccati equation X⋉A⋉X=B has a unique positive solution X=A−1♯1/2B.
More generally, consider the following symmetric word equation in two positive definite letters A,B∈Pn with respect to the usual products:
B=XAXAX⋯AXAX((p+1)-terms of X, and p-terms of A)=X(AX)p, |
here p∈N. We now investigate such equations with respect to semi-tensor products.
Corollary 5.2. Let A∈Pm and B,X∈Pn with A≺kB.
(1). Let p∈N. Then the symmetric word equation
X(A⋉X)p=B | (5.2) |
is uniquely solvable with an explicit solution X=A−1♯1p+1B.
(2). Let r∈R−{−1}. Then the symmetric word equation
X(X⋉A⋉X)rX=B | (5.3) |
is uniquely solvable with an explicit solution
X=(A−1♯1r+1B)1/2. |
Proof. First, since p∈N, we can observe the following:
X(A⋉X)p=X1/2(X1/2⋉A⋉X1/2)pX1/2. |
It follows from the results in Section 3 that
X(A⋉X)p=X1/2(X−1/2⋉A−1⋉X−1/2)−pX1/2=X♯−pA−1=A−1♯p+1X. |
According to Corollary 4.1, the equation A−1♯p+1X=B has a unique solution X=A−1♯1p+1B.
To solve Eq (5.3), we observe the following:
X(X⋉A⋉X)rX=X(X−1⋉A−1⋉X−1)−rX=X2♯−rA−1=A−1♯r+1X2. |
According to Corollary 4.1, the equation A−1♯r+1X2=B has a unique solution X2=A−1♯1r+1B. Hence, we get the desire formula of X.
We extend the notion of the classical weighted MGM to that of positive definite matrices of arbitrary dimensions, so that the usual matrix products are generalized to the semi-tensor products. When the weights are arbitrary real numbers, the weighted MGMs posses not only nice properties as in the classical case, e.g. the congruent invariance and the self duality, but also affine change of parameters, exponential law, and left/right cancellability. Moreover, when the weights belong to the unit interval, the weighted MGM has remarkable properties, namely, monotonicity and continuity from above (according to the famous Löwner-Heinz inequality). When the matrix A or B is not assumed to be invertible, we can define A♯tB where the weight t is restricted to [0,∞) or (−∞,1]. Then we apply a continuity argument to extend the weighted MGM to positive semidefinite matrices, here the weights belong to the unit interval. It turns out that this matrix mean posses rich algebraic, order, and analytic properties, such as, monotonicity, continuity from above, congruent invariance, permutation invariance, affine change of parameters, and exponential law. Furthermore, we investigate certain equations concerning weighted MGMs of positive definite matrices. Due to the cancellability and another properties of the weighted MGM, such equations are always uniquely solvable with solutions expressed in terms of weighted MGMs. The notion of MGMs can be applied to solve certain symmetric word equations in two positive definite letters. A particular interest of the word equations in the field of control engineering is the Riccati equation in a general form involving semi-tensor products. Our results include the classical weighted MGMs of matrices as special case.
The authors declare they have not used Artificial Intelligence (AI) tools in the creation of this article.
This research is supported by postdoctoral fellowship of School of Science, King Mongkut's Institute of Technology Ladkrabang. The authors thank anonymous referees for their comments and suggestions on the manuscript.
The authors declare there is no conflicts of interest.
[1] |
Carr C, de Oliveira B, Jackson S, et al. (2022) Identification of BgP, a cutinase-like polyesterase from a deep-sea sponge-derived Actinobacterium. Front Microbiol 13: 888343. https://doi.org/10.3389/fmicb.2022.888343 ![]() |
[2] |
Dalmaso G, Ferreira D, Vermelho A (2015) Marine extremophiles: a source of hydrolases for biotechnological applications. Mar Drugs 13: 1925-1965. https://doi.org/10.3390/md13041925 ![]() |
[3] |
Rosenberg E, Zilber-Rosenberg I (2018) The hologenome concept of evolution after 10 years. Microbiome 6: 1-14. https://doi.org/10.1186/s40168-018-0457-9 ![]() |
[4] |
de Oliveira B, Carr C, Dobson A, et al. (2020) Harnessing the sponge microbiome for industrial biocatalysts. Appl Microbiol Biotechnol 10: 8131-8154. https://doi.org/10.1007/s00253-020-10817-3 ![]() |
[5] |
Arnosti C, Bell C, Moorhead D, et al. (2014) Extracellular enzymes in terrestrial, freshwater, and marine environments: perspectives on system variability and common research needs. Biogeochemistry 117: 5-21. https://doi.org/10.1007/s10533-013-9906-5 ![]() |
[6] | PlasticsEuropePlastics–The Facts 2022: An Analysis of European plastics production, demand, and waste (2023). Available from: https://plasticseurope.org/knowledge-hub/plastics-the-facts-2022/. |
[7] |
Jambeck J, Geyer R, Wilcox C, et al. (2015) Plastic waste inputs from land into the ocean. Science 347: 768-771. https://doi.org/10.1126/science.1260352 ![]() |
[8] |
Oberbeckmann S, Osborn A, Duhaime M (2016) Microbes on a bottle: substrate, season and geography influence community composition of microbes colonizing marine plastic debris. PLoS One 11: e0159289. https://doi.org/10.1371/journal.pone.0159289 ![]() |
[9] |
Cox K, Covernton G, Davies H, et al. (2019) Human consumption of microplastics. Environ Sci Technol 53: 7068-7074. https://doi.org/10.1021/acs.est.9b01517 ![]() |
[10] |
Gregory M (2009) Environmental implications of plastic debris in marine settings entanglement, ingestion, smothering, hangers-on, hitch-hiking and alien invasions. Phil Trans R Soc B 364: 2013-2025. https://doi.org/10.1098/rstb.2008.0265 ![]() |
[11] |
Worm B, Lotze H, Jubinville I, et al. (2017) Plastic as a persistent marine pollutant. Annu Rev Environ Resour 42: 1-26. https://doi.org/10.1146/annurev-environ-102016-060700 ![]() |
[12] |
Carlton J, Fowler A (2018) Ocean rafting and marine debris: A broader vector menu requires a greater appetite for invasion biology research support. Aquat Invasions 13: 11-15. https://doi.org/10.3391/ai.2018.13.1.02 ![]() |
[13] |
Tetu S, Sarker I, Moore L (2020) How will marine plastic pollution affect bacterial primary producers?. Commun Biol 3: 1-4. https://doi.org/10.1038/s42003-020-0789-4 ![]() |
[14] |
Bowley J, Baker–Austin C, Porter A, et al. (2021) Oceanic hitchhikers–assessing pathogen risks from marine microplastic. Trends Microbiol 29: 107-116. https://doi.org/10.1016/j.tim.2020.06.011 ![]() |
[15] |
Pirillo V, Pollegioni L, Molla G (2021) Analytical methods for the investigation of enzyme–catalyzed degradation of polyethylene terephthalate. FEBS J 288: 4730-4745. https://doi.org/10.1111/febs.15850 ![]() |
[16] |
Koshti R, Mehta L, Samarth N (2018) Biological recycling of polyethylene terephthalate: A mini–review. J Polym Environ 26: 3520-3529. https://doi.org/10.1007/s10924-018-1214-7 ![]() |
[17] | Zimmermann W (2019) Biocatalytic recycling of polyethylene terephthalate plastic. Philos Trans R Soc A: 378. https://doi.org/10.1098/rsta.2019.0273 |
[18] |
Dissanayake L, Jayakody L (2021) Engineering microbes to bio-upcycle Polyethylene Terephthalate. Front Bioeng Biotechnol 9: 656465. https://doi.org/10.3389/fbioe.2021.656465 ![]() |
[19] |
Tiso T, Narancic T, Wei R, et al. (2021) Towards bio-upcycling of polyethylene terephthalate. Metab Eng 66: 167-178. https://doi.org/10.1016/j.ymben.2021.03.011 ![]() |
[20] |
Danso D, Chow J, Streit W (2019) Plastics: Environmental and biotechnological perspectives on microbial degradation. Appl Environ Microbiol 85: 01019-010195. https://doi.org/10.1128/AEM.01095-19 ![]() |
[21] |
Schmidt J, Wei R, Oeser T (2017) Degradation of polyester polyurethane by bacterial polyester hydrolases. Polymers 9: 65. https://doi.org/10.3390/polym9020065 ![]() |
[22] |
Carr C, Clarke D, Dobson A (2020) Microbial polyethylene terephthalate hydrolases: current and future perspectives. Front Microbiol 11: 1-23. https://doi.org/10.3389/fmicb.2020.571265 ![]() |
[23] |
Mohanan N, Montazer Z, Sharma P, et al. (2020) Microbial and enzymatic degradation of synthetic plastics. Front Microbiol 11: 580709. https://doi.org/10.3389/fmicb.2020.580709 ![]() |
[24] |
Ru J, Huo Y, Yang Y (2020) Microbial degradation and valorization of plastic wastes. Front Microbiol 11: 442. https://doi.org/10.3389/fmicb.2020.00442 ![]() |
[25] |
Kawai F, Kawabata T, Oda M (2019) Current knowledge on enzymatic PET degradation and its possible application to waste stream management and other fields. Appl Microbiol Biotechnol 103: 4253-4268. https://doi.org/10.1007/s00253-019-09717-y ![]() |
[26] |
Danso D, Schmeisser C, Chow J, et al. (2018) New insights into the function and global distribution of polyethylene terephthalate (PET)-degrading bacteria and enzymes in marine and terrestrial metagenomes. Appl Environ Microbiol 84: e02773-17. https://doi.org/10.1128/AEM.02773-17 ![]() |
[27] |
Müller R, Schrader H, Profe J, et al. (2005) Enzymatic degradation of poly (ethylene terephthalate): Rapid Hydrolysis using a hydrolase from T. fusca. Macromol Rapid Commun 26: 1400-1405. https://doi.org/10.1002/marc.200500410 ![]() |
[28] |
Yoshida S, Hiraga K, Takehana T, et al. (2016) A bacterium that degrades and assimilates poly (ethylene terephthalate). Science 351: 1196-1199. https://doi.org/10.1126/science.aad6359 ![]() |
[29] |
Ekanayaka A, Tibpromma S, Dai D, et al. (2022) A review of the fungi that degrade plastic. J Fungi 8: 772. https://doi.org/10.3390/jof8080772 ![]() |
[30] |
Roth C, Wei R, Oeser T, et al. (2014) Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca. Appl Microbiol Biotechnol 98: 7815-7823. https://doi.org/10.1007/s00253-014-5672-0 ![]() |
[31] |
Sulaiman S, Yamato S, Kanaya E, et al. (2012) Isolation of a novel cutinase homolog with polyethylene terephthalate–degrading activity from leaf–branch compost by using a metagenomic approach. Appl Environ Microbiol 78: 1556-1562. https://doi.org/10.1128/AEM.06725-11 ![]() |
[32] |
Then J, Wei R, Oeser T, et al. (2016) A disulfide bridge in the calcium binding site of a polyester hydrolase increases its thermal stability and activity against polyethylene terephthalate. FEBS Open Bio 6: 425-432. https://doi.org/10.1002/2211-5463.12053 ![]() |
[33] |
Gambarini V, Pantos O, Kingsbury J, et al. (2021) Phylogenetic distribution of plastic-degrading microorganisms. mSystems 6: e01112-20. https://doi.org/10.1128/mSystems.01112-20 ![]() |
[34] |
Imhoff J (2005) Enterobacteriales. Bergey's manual® of systematic bacteriology . Springer 587-850. https://doi.org/10.1007/0-387-28022-7_13 ![]() |
[35] | Brenner D, Farmer J (2005) III. Family Enterobacteriaceae. Bergey's manual® of systematic bacteriology . Springer 587-606. https://doi.org/10.1002/9781118960608.fbm00222 |
[36] |
Janda J, Abbott S (2021) The changing face of the family Enterobacteriaceae (Order: “Enterobacterales”): New members, taxonomic issues, geographic expansion, and new diseases and disease syndromes. Clin Microbiol Rev 34: 1-45. https://doi.org/10.1128/CMR.00174-20 ![]() |
[37] |
Kato C, Honma A, Sato S, et al. (2019) Poly 3-hydroxybutyrate-co- 3-hydroxyhexanoate films can be degraded by the deep-sea microbes at high pressure and low temperature conditions. High Press Res 39: 248-257. https://doi.org/10.1080/08957959.2019.1584196 ![]() |
[38] |
Borchert E, García-Moyano A, Sanchez-Carrillo S, et al. (2021) Deciphering a marine bone-degrading microbiome reveals a complex community effort. mSystems 6: 1218-20. https://doi.org/10.1128/mSystems.01218-20 ![]() |
[39] |
Yang J, Yang Y, Wu W, et al. (2014) Evidence of polyethylene biodegradation by bacterial strains from the guts of plastic-eating waxworms. Environ Sci Technol 48: 13776-13784. https://doi.org/10.1021/es504038a ![]() |
[40] |
Mallakuntla M, Vaikuntapu P, Bhuvanachandra B, et al. (2017) Transglycosylation by a chitinase from Enterobacter cloacae subsp. cloacae generates longer chitin oligosaccharides. Sci Rep 7: 1-12. https://doi.org/10.1038/s41598-017-05140-3 ![]() |
[41] |
Volova T, Boyandin A, Vasil'ev A, et al. (2011) Biodegradation of polyhydroxyalkanoates (PHAs) in the South China Sea and identification of PHA-degrading bacteria. Microbiology 80: 252-260. https://doi.org/10.1134/S0026261711020184 ![]() |
[42] |
Dashti N, Ali N, Eliyas M, et al. (2015) Most hydrocarbonoclastic bacteria in the total environment are diazotrophic, which highlights their value in the bioremediation of hydrocarbon contaminants. Microbes Environ 30: 70-75. https://doi.org/10.1264/jsme2.ME14090 ![]() |
[43] |
Wang X, Isbrandt T, Strube M, et al. (2021) Chitin degradation machinery and secondary metabolite profiles in the marine bacterium Pseudoalteromonas rubra S4059. Mar Drugs 19: 108. https://doi.org/10.3390/md19020108 ![]() |
[44] |
Caruso G (2020) Microbial colonization in marine environments: overview of current knowledge and emerging research topics. J Mar Sci Eng 8: 78. https://doi.org/10.3390/jmse8020078 ![]() |
[45] |
Sekiguchi T, Saika A, Nomura K, et al. (2011) Biodegradation of aliphatic polyesters soaked in deep seawaters and isolation of poly(ϵ-caprolactone)-degrading bacteria. Poly. Degrad Stabil 96: 1397-1403. https://doi.org/10.1016/j.polymdegradstab.2011.03.004 ![]() |
[46] |
Ohta Y, Hatada Y, Miyazaki M, et al. (2005) Purification and characterization of a novel α-agarase from a Thalassomonas sp. Curr Microbiol 50: 212-216. https://doi.org/10.1007/s00284-004-4435-z ![]() |
[47] |
Yakimov M, Bargiela R, Golyshin P (2022) Calm and Frenzy: marine obligate hydrocarbonoclastic bacteria sustain ocean wellness. Curr Opin Biotechnol 73: 337-345. https://doi.org/10.1016/j.copbio.2021.09.015 ![]() |
[48] |
Molitor R, Bollinger A, Kubicki S, et al. (2020) Agar platebased screening methods for the identification of polyester hydrolysis by Pseudomonas species. Microb Biotechnol 13: 274-284. https://doi.org/10.1111/1751-7915.13418 ![]() |
[49] |
Pérez-García P, Danso D, Zhang H, et al. (2021) Exploring the global metagenome for plastic-degrading enzymes. Methods Enzymol 648: 137-157. https://doi.org/10.1016/bs.mie.2020.12.022 ![]() |
[50] | Genome Taxonomy Database (GTDB)University of Queensland (2023). Available from: https://gtdb.ecogenomic.org/. |
[51] | R Studio Team (2020). Available from: https://support--rstudio-com.netlify.app/. |
[52] |
Noda T, Sagara H, Yen A, et al. (2006) Architecture of ribonucleoprotein complexes in influenza A virus particles. Nature 439: 490-492. https://doi.org/10.1038/nature04378 ![]() |
[53] |
Reysenbach A, Longnecker K, Kirshtein J (2000) Novel bacterial and archaeal lineages from an in situ growth chamber deployed at a mid-atlantic ridge hydrothermal vent. Appl Environ Microbiol 66: 3798-3806. https://doi.org/10.1128/AEM.66.9.3798-3806.2000 ![]() |
[54] |
Kumar S, Stecher G, Li M, et al. (2018) MEGA X: Molecular evolutionary genetics analysis across computing platforms. Mol Biol Evol 35: 1547-1549. https://doi.org/10.1093/molbev/msy096 ![]() |
[55] |
Larkin M, Blackshields G, Brown N, et al. (2007) Clustal W and Clustal X version 2.0. Bioinformatics 23: 2947-2948. https://doi.org/10.1093/bioinformatics/btm404 ![]() |
[56] |
Price M, Dehal P, Arkin A (2009) Fasttree: Computing large minimum evolution trees with profiles instead of a distance matrix. Mol Biol Evol 26: 1641-1650. https://doi.org/10.1093/molbev/msp077 ![]() |
[57] |
Price M, Dehal P, Arkin A (2010) FastTree 2-Approximately maximum-likelihood trees for large alignments. PLoS One 5: e9490. https://doi.org/10.1371/journal.pone.0009490 ![]() |
[58] | ITOL, Interactive Tree Of Life. Available from: https://itol.embl.de. |
[59] |
Letunic I, Bork P (2021) Interactive Tree Of Life (iTOL) v5: an online tool for phylogenetic tree display and annotation. Nucleic Acids Res 49: 293-296. https://doi.org/1093/nar/gkab301 ![]() |
[60] | Desjardins P, Conklin D (2010) NanoDrop microvolume quantitation of nucleic acids. J Vis Exp 45: e2565. https://doi.org/10.3791/2565 |
[61] |
Kolmogorov M, Yuan J, Lin Y, et al. (2019) Assembly of long, error-prone reads using repeat graphs. Nat Biotechnol 37: 540-546. https://doi.org/10.1038/s41587-019-0072-8 ![]() |
[62] |
Parks D, Chuvochina M, Waite D, et al. (2018) A standardized bacterial taxonomy based on genome phylogeny substantially revises the tree of life. Nat Biotechnol 36: 996-1004. https://doi.org/10.1038/nbt.4229 ![]() |
[63] |
Chaumeil P, Mussig A, Hugenholtz P, et al. (2019) GTDB-Tk: a toolkit to classify genomes with the Genome Taxonomy Database. Bioinformatics 36: 1925-1927. https://doi.org/10.1093/bioinformatics/btz848 ![]() |
[64] |
Hyatt D (2010) Prodigal: prokaryotic gene recognition and translation initiation site identification. BMC Bioinformatics 11: 119-119. https://doi.org/10.1186/1471-2105-11-119 ![]() |
[65] |
Eddy S (2011) Accelerated profile HMM searches. PLoS Comput Biol 7: e1002195. https://doi.org/10.1371/journal.pcbi.1002195 ![]() |
[66] |
Matsen F, Kodner R, Armbrust E (2010) pplacer: linear time maximum-likelihood and Bayesian phylogenetic placement of sequences onto a fixed reference tree. BMC Bioinformatics 11: 538. https://doi.org/10.1186/1471-2105-11-538 ![]() |
[67] |
Huerta-Cepas J, Szklarczyk D, Heller D, et al. (2019) Eggnog 5.0: a hierarchical, functionally and phylogenetically annotated orthology resource based on 5090 organisms and 2502 viruses. Nucleic Acids Res 47: 309-314. https://doi.org/nar/gky1085 ![]() |
[68] |
Almeida E, Carrillo Rincón A, Jackson S, et al. (2019) In silico screening and heterologous expression of a polyethylene terephthalate hydrolase (PETase)-like enzyme (SM14est) with polycaprolactone (PCL)-degrading activity, from the marine sponge-derived strain Streptomyces sp. SM14. Front Microbiol 10: 2187. https://doi.org/10.3389/fmicb.2019.02187 ![]() |
[69] |
Buchholz P, Feuerriegel G, Zhang H, et al. (2022) Plastics degradation by hydrolytic enzymes: The plastics-active enzymes database—PAZy. Proteins: Structure, Function, and Bioinformatics. Proteins 90: 1443-1456. https://doi.org/10.1002/prot.26325 ![]() |
[70] |
Di Tommaso P, Moretti S, Xenarios I, et al. (2011) T-Coffee: a web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension. Nucleic Acids Res 39: 13-17. https://doi.org/10.1093/nar/gkr245 ![]() |
[71] |
Gouet P, Courcelle E, Stuart D, et al. (1999) Espript: analysis of multiple sequence alignments in Postscript. Bioinformatics 15: 305-308. https://doi.org/10.1093/bioinformatics/15.4.305 ![]() |
[72] | The Lipase Engineering Database (LED) version4.1.0. Germany: University of Stuttgart. Available from: https://led.biocatnet.de/. |
[73] |
Armenteros J, Tsirigos K, Sønderby C, et al. (2019) SignalP 5.0 improves signal peptide predictions using deep neural networks. Nat Biotechnol 37: 420-423. https://doi.org/10.1038/s41587-019-0036-z ![]() |
[74] |
Baek M, DiMaio F, Anishchenko I, et al. (2021) Accurate prediction of protein structures and interactions using a three-track neural network. Science 373: 871-876. https://doi.org/10.1126/science.abj8754 ![]() |
[75] |
Blázquez-Sánchez P, Engelberger F, Cifuentes-Anticevic J, et al. (2022) Antarctic polyester hydrolases degrade aliphatic and aromatic polyesters at moderate temperatures. Appl Environ Microbiol 88: e0184221. https://doi.org/10.1128/AEM.01842-21 ![]() |
[76] |
Bollinger A, Thies S, Knieps-Grünhagen E, et al. (2020) A novel polyester hydrolase from the marine bacterium Pseudomonas aestusnigri–structural and functional insights. Front Microbiol 11: 1-16. https://doi.org/10.3389/fmicb.2020.00114 ![]() |
[77] |
Ronkvist Å, Xie W, Lu W, et al. (2009) Cutinase-catalyzed hydrolysis of poly (ethylene terephthalate). Macromolecules 42: 5128-5138. https://doi.org/10.1021/ma9005318 ![]() |
[78] | Eiamthong B, Meesawat P, Wongsatit T, et al. (2022) Discovery and genetic code expansion of a polyethylene terephthalate (PET) hydrolase from the human saliva metagenome for the degradation and bio-functionalization of PET. Angew Chem 61: e202203061. https://doi.org/10.1002/anie.202203061 |
[79] |
Wallace P, Haernvall K, Ribitsch D, et al. (2017) PpEst is a novel PBAT degrading polyesterase identified by proteomic screening of Pseudomonas pseudoalcaligenes. Appl Microbiol Biotechnol 101: 2291-2303. https://doi.org/10.1007/s00253-016-7992-8 ![]() |
[80] |
Martínez-Tobón D, Gul M, Elias A, et al. (2018) Polyhydroxybutyrate (PHB) biodegradation using bacterial strains with demonstrated and predicted PHB depolymerase activity. Appl Microbiol Biotechnol 102: 8049-8067. https://doi.org/10.1007/s00253-018-9153-8 ![]() |
[81] |
Liu X, Hille P, Zheng M, et al. (2019) Diversity of polyester degrading bacteria in surface sediments from Yangtze River Estuary. AIP Conf Proc 2122: 020063. https://doi.org/10.1063/1.5116502 ![]() |
[82] |
Qiu L, Yin X, Liu T, et al. (2020) Biodegradation of bis (2-hydroxyethyl) terephthalate by a newly isolated Enterobacter sp. HY1 and characterization of its esterase properties. J Basic Microbiol 60: 699-711. https://doi.org/10.1002/jobm.202000053 ![]() |
[83] |
Gaino E, Pronzato R (1989) Ultrastructural evidence of bacterial damage to Spongia officinalis fibres (Porifera, Demospongiae). Dis Aquat Organ 6: 67-74. https://www.int-res.com/articles/dao/6/d006p067.pdf ![]() |
[84] |
Reisser J, Shaw J, Hallegraeff G, et al. (2014) Millimeter-sized marine plastics: a new pelagic habitat for microorganisms and invertebrates. PloS One 9: e100289. https://doi.org/10.1371/journal.pone.0100289 ![]() |
[85] |
Bryant J, Clemente T, Viviani D, et al. (2016) Diversity and activity of communities inhabiting plastic debris in the North Pacific Gyre. mSystems 1: 024-16. https://doi.org/10.1128/mSystems.00024-16 ![]() |
[86] |
Kiessling T, Gutow L, Thiel M (2015) Marine litter as habitat and dispersal vector. Marine anthropogenic litter . Cham: Springer Open Elsevier 141-181. https://doi.org/10.1007/978-3-319-16510-3_6 ![]() |
[87] |
Zelezniak A, Andrejev S, Ponomarova O, et al. (2015) Metabolic dependencies drive species co-occurrence in diverse microbial communities. Proc Natl Acad Sci 112: 6449-6454. https://doi.org/10.1073/pnas.1421834112 ![]() |
[88] |
Borchert E, Hammerschmidt K, Hentschel U, et al. (2021) Enhancing microbial pollutant degradation by integrating eco-evolutionary principles with environmental biotechnology. Trends Microbiol 29: 908-918. https://doi.org/10.1016/j.tim.2021.03.002 ![]() |
[89] |
Tournier V, Topham C, Gilles A, et al. (2020) An engineered PET depolymerase to break down and recycle plastic bottles. Nature 580: 216-219. https://doi.org/10.1038/s41586-020-2149-4 ![]() |
[90] |
Lenfant N, Hotelier T, Bourne Y, et al. (2013) Proteins with an alpha/beta hydrolase fold: relationships between subfamilies in an ever-growing superfamily. Chem Biol Interact 203: 266-268. https://doi.org/10.1016/j.cbi.2012.09.003 ![]() |
[91] |
Gricajeva A, Nadda A, Gudiukaite R (2021) Insights into polyester plastic biodegradation by carboxyl ester hydrolases. J Chem Technol Biotechnol 97: 359-380. https://doi.org/10.1002/jctb.6745 ![]() |
![]() |
![]() |
1. | Shaher Momani, Iqbal M. Batiha, Amira Abdelnebi, Iqbal H. Jebril, A powerful tool for dealing with high-dimensional fractional-order systems with applications to fractional Emden–Fowler systems, 2024, 12, 25900544, 100110, 10.1016/j.csfx.2024.100110 | |
2. | Rongpu Sun, Zhanbing Bai, Existence of solutions to a system of fractional three-point boundary value problem at resonance, 2024, 470, 00963003, 128576, 10.1016/j.amc.2024.128576 | |
3. | K. Venkatachalam, M. Sathish Kumar, P. Jayakumar, Results on non local impulsive implicit Caputo-Hadamard fractional differential equations, 2024, 4, 2767-8946, 286, 10.3934/mmc.2024023 | |
4. | Abduljawad Anwar, Shayma Adil Murad, On the Ulam stability and existence of Lp-solutions for fractional differential and integro-differential equations with Caputo-Hadamard derivative, 2024, 4, 2767-8946, 439, 10.3934/mmc.2024035 | |
5. | Abdulrahman A. Sharif, Maha M. Hamood, Ahmed A. Hamoud, Kirtiwant P. Ghadle, Novel results on impulsive Caputo–Hadamard fractional Volterra–Fredholm integro-differential equations with a new modeling integral boundary value problem, 2025, 16, 1793-9623, 10.1142/S1793962325500333 | |
6. | Mengyan Ge, Kai Jia, Xin Wang, Yujie Liu, Yuqi Jiang, Researches on dynamics and noise effects of FHN neuron based on memristor–memcapacitor coupling, 2025, 0924-090X, 10.1007/s11071-025-11454-z |