Abstract:
: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.
journal_name
Macromol Bioscijournal_title
Macromolecular bioscienceauthors
Hiraishi T,Masuda E,Kanayama N,Nagata M,Doi Y,Abe H,Maeda Mdoi
10.1002/mabi.200800106subject
Has Abstractpub_date
2009-01-09 00:00:00pages
10-9issue
1eissn
1616-5187issn
1616-5195journal_volume
9pub_type
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