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Applied and Environmental Microbiology, May 2003, p. 2498-2504, Vol. 69, No. 5
0099-2240/03/$08.00+0 DOI: 10.1128/AEM.69.5.2498-2504.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
PRESTO, Japan Science and Technology Corporation,1 Institute of Applied Biochemistry, University of Tsukuba, Tsukuba, Ibaraki 305-8572, Japan,2 Institute of Agricultural Technology, School of Biotechnology, Suranaree University of Technology, Nakhon-Ratchasima, Thailand 300003
Received 4 November 2002/ Accepted 24 January 2003
The gene encoding a poly(DL-lactic acid) (PLA) depolymerase from Paenibacillus amylolyticus strain TB-13 was cloned and overexpressed in Escherichia coli. The purified recombinant PLA depolymerase, PlaA, exhibited degradation activities toward various biodegradable polyesters, such as poly(butylene succinate), poly(butylene succinate-co-adipate), poly(ethylene succinate), and poly(
-caprolactone), as well as PLA. The monomeric lactic acid was detected as the degradation product of PLA. The substrate specificity toward triglycerides and p-nitrophenyl esters indicated that PlaA is a type of lipase. The gene encoded 201 amino acid residues, including the conserved pentapeptide Ala-His-Ser-Met-Gly, present in the lipases of mesophilic Bacillus species. The identity of the amino acid sequence of PlaA with Bacillus lipases was no more than 45 to 50%, and some of its properties were different from those of these lipases.
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