Cloning of Poly(aspartic acid) (PAA) Hydrolase-1 Gene from Pedobacter sp KP-2 and Hydrolysis of Thermally Synthesized PAA by its Gene Product

被引：11

作者：

Hiraishi, Tomohiro ^{[1
]}

Masuda, Eriko ^{[1
,2
]}

Kanayama, Naoki ^{[1
]}

Nagata, Madoka ^{[3
]}

Doi, Yoshiharu ^{[3
]}

Abe, Hideki ^{[2
,3
]}

Maeda, Mizuo ^{[1
]}

机构：

[1] Riken Inst Phys & Chem Res, Bioengn Lab, Wako, Saitama 3510198, Japan

[2] Tokyo Inst Technol, Dept Innovat & Engn Mat, Midori Ku, Kanagawa 2268502, Japan

[3] Riken Inst Phys & Chem Res, Polymer Chem Lab, Wako, Saitama 3510198, Japan

来源：

MACROMOLECULAR BIOSCIENCE | 2009年 / 9卷 / 01期

关键词：

beta-aspartic acid; biodegradable; pedobacter sp KP-2; poly(aspartic acid) hydrolase; water-soluble polymers; SPHINGOMONAS SP KT-1; L-ASPARTIC ACID; ESCHERICHIA COLI; POLY(SUCCINIMIDE); BIODEGRADABILITY; POLYCONDENSATION; POLYASPARTATE; PURIFICATION; DEGRADATION; PHOSPHATASE;

D O I：

10.1002/mabi.200800106

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pedobacter sp. KP-2 can degrade and metabolize thermally synthesized alpha,beta-poly(D,L-aspartic acid) (tPAA), which contains 70% of unnatural beta-amide units, with high-molecular-weight. In this study, gene cloning and molecular characterization of PAA hydrolase-1 from KP-2 was carried out. Gene analysis reveals that deduced amino acid sequence of the enzyme shows a similarity to only that of PAA hydrolase-1 from Sphingomonas sp. KT-1. GPC and NMR analyses of the hydrolyzed products of tPAA by PAA hydrolase-1 of KP-2 indicate that this enzyme cleaves the beta-beta amide linkage via endo-mode to yield oligo(aspartic acid) from tPAA. Taking the composition of tPAA and the substrate specificity of PAA hydrolase-1 into consideration, the enzyme possibly plays a crucial role in tPAA biodegradation by KP-2.

引用

页码：10 / 19

页数：10