Cloning of Poly(aspartic acid) (PAA) Hydrolase-1 Gene from Pedobacter sp. KP-2 and Hydrolysis of Thermally Synthesized PAA by its Gene Product
✍ Scribed by Tomohiro Hiraishi; Eriko Masuda; Naoki Kanayama; Madoka Nagata; Yoshiharu Doi; Hideki Abe; Mizuo Maeda
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 440 KB
- Volume
- 9
- Category
- Article
- ISSN
- 1616-5187
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✦ Synopsis
Abstract
Pedobacter sp. KP‐2 can degrade and metabolize thermally synthesized α,β‐poly(D,L‐aspartic acid) (tPAA), which contains 70% of unnatural β‐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 β‐β 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.
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