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从海洋微生物群落中分离出的串联和冷适应PET水解酶Ple628和Ple629的分子与生化差异

Molecular and Biochemical Differences of the Tandem and Cold-Adapted PET Hydrolases Ple628 and Ple629, Isolated From a Marine Microbial Consortium.

作者信息

Meyer Cifuentes Ingrid E, Wu Pan, Zhao Yipei, Liu Weidong, Neumann-Schaal Meina, Pfaff Lara, Barys Justyna, Li Zhishuai, Gao Jian, Han Xu, Bornscheuer Uwe T, Wei Ren, Öztürk Başak

机构信息

Junior Research Group Microbial Biotechnology, Leibniz Institute DSMZ-German Collection of Microorganisms and Cell Cultures, Braunschweig, Germany.

Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, China.

出版信息

Front Bioeng Biotechnol. 2022 Jul 21;10:930140. doi: 10.3389/fbioe.2022.930140. eCollection 2022.

DOI:10.3389/fbioe.2022.930140
PMID:35935485
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9350882/
Abstract

Polybutylene adipate terephthalate (PBAT) is a biodegradable alternative to polyethylene and can be broadly used in various applications. These polymers can be degraded by hydrolases of terrestrial and aquatic origin. In a previous study, we identified tandem PETase-like hydrolases (Ples) from the marine microbial consortium I1 that were highly expressed when a PBAT blend was supplied as the only carbon source. In this study, the tandem Ples, Ple628 and Ple629, were recombinantly expressed and characterized. Both enzymes are mesophilic and active on a wide range of oligomers. The activities of the Ples differed greatly when model substrates, PBAT-modified polymers or PET nanoparticles were supplied. Ple629 was always more active than Ple628. Crystal structures of Ple628 and Ple629 revealed a structural similarity to other PETases and can be classified as member of the PETases IIa subclass, α/β hydrolase superfamily. Our results show that the predicted functions of Ple628 and Ple629 agree with the bioinformatic predictions, and these enzymes play a significant role in the plastic degradation by the consortium.

摘要

聚己二酸对苯二甲酸丁二醇酯(PBAT)是聚乙烯的一种可生物降解替代品,可广泛应用于各种领域。这些聚合物可被陆生和水生来源的水解酶降解。在之前的一项研究中,我们从海洋微生物群落I1中鉴定出串联的类PETase水解酶(Ples),当以PBAT共混物作为唯一碳源时,这些酶会高度表达。在本研究中,对串联Ples,即Ple628和Ple629进行了重组表达和特性分析。这两种酶都是嗜温酶,对多种低聚物都有活性。当提供模型底物、PBAT改性聚合物或PET纳米颗粒时,Ples的活性差异很大。Ple629总是比Ple628更具活性。Ple628和Ple629的晶体结构显示出与其他PETase的结构相似性,可归类为PETases IIa亚类、α/β水解酶超家族的成员。我们的结果表明,Ple628和Ple629的预测功能与生物信息学预测一致,并且这些酶在该群落的塑料降解中发挥着重要作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/88aad1085a2a/fbioe-10-930140-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/07b8c1f49141/fbioe-10-930140-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/938a046bb88d/fbioe-10-930140-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/9e8faad7afe3/fbioe-10-930140-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/f95220c75923/fbioe-10-930140-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/287e484698d7/fbioe-10-930140-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/88aad1085a2a/fbioe-10-930140-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/07b8c1f49141/fbioe-10-930140-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/938a046bb88d/fbioe-10-930140-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/9e8faad7afe3/fbioe-10-930140-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/f95220c75923/fbioe-10-930140-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/287e484698d7/fbioe-10-930140-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8642/9350882/88aad1085a2a/fbioe-10-930140-g006.jpg

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