Poly(aspartic acid) (PAA) hydrolases and PAA biodegradation: current knowledge and impact on applications

被引：19
作者：
Hiraishi, Tomohiro [1 ,2 ]
机构：
[1] RIKEN, Bioengn Lab, 2-1 Hirosawa, Wako, Saitama 3510198, Japan
[2] RIKEN, CSRS, Biomass Engn Res Div, Bioplast Res Team, 2-1 Hirosawa, Wako, Saitama 3510198, Japan
来源：
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 2016年 / 100卷 / 04期
关键词：
Poly(aspartic acid); Poly(aspartic acid) hydrolase; beta-Amide linkage; Stereoselectivity; Enzyme-catalyzed polymerization; BETA-PEPTIDYL AMINOPEPTIDASES; SPHINGOMONAS SP KT-1; L-GLUTAMIC ACID; DIETHYL ESTER; ENZYMATIC-HYDROLYSIS; MICROBIAL-DEGRADATION; PEDOBACTER SP; AMINO-ACIDS; PROTEASE; POLYMERIZATION;
D O I：
10.1007/s00253-015-7216-7
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Thermally synthesized poly(aspartic acid) (tPAA) is a bio-based, biocompatible, biodegradable, and water-soluble polymer that has a high proportion of beta-Asp units and equivalent moles of D- and L-Asp units. Poly(aspartic acid) (PAA) hydrolase-1 and hydrolase-2 are tPAA biodegradation enzymes purified from Gram-negative bacteria. PAA hydrolase-1 selectively cleaves amide bonds between beta-Asp units via an endo-type process, whereas PAA hydrolase-2 catalyzes the exo-type hydrolysis of the products of tPAA hydrolysis by PAA hydrolase-1. The novel reactivity of PAA hydrolase-1 makes it a good candidate for a biocatalyst in beta-peptide synthesis. This mini-review gives an overview of PAA hydrolases with emphasis on their biochemical and functional properties, in particular, PAA hydrolase-1. Functionally related enzymes, such as poly(R-3-hydroxybutyrate) depolymerases and beta-aminopeptidases, are compared to PAA hydrolases. This mini-review also provides findings that offer an insight into the catalytic mechanisms of PAA hydrolase-1 from Pedobacter sp. KP-2.
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收藏
页码：1623 / 1630
页数：8
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