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Characterization of an extracellular poly(3-hydroxyoctanoate) depolymerase from the marine isolate, Pseudomonasluteola M13-4

Paper ID Volume ID Publish Year Pages File Format Full-Text
18798 42743 2006 7 PDF Available
Title
Characterization of an extracellular poly(3-hydroxyoctanoate) depolymerase from the marine isolate, Pseudomonasluteola M13-4
Abstract

The characteristics of an extracellular poly(3-hydroxyoctanoate) (PHO) depolymerase purified from the marine isolate Pseudomonas luteola M13-4 were elucidated. The enzyme consisted of a monomeric subunit, having a molecular mass of 28 kDa and isoelectric point of 6.0. The optimum reaction pH and temperature were 10.0 and 40 °C, respectively. Its hydrolyzing activity was significantly inhibited by phenylmethylsulfonyl fluoride (PMSF), suggesting the involvement of a serine as an active site amino acid. The enzyme was able to hydrolyze various types of medium-chain-length poly(3-hydroxyalkanoates) (MCL-PHAs) as well as various chain-length p-nitrophenyl (PNP) esters of fatty acids. The amino acid sequence of the tryptic peptide contained a lipase box pentapeptide sequence, G-I-S-S-G. The N-terminal amino acid sequence of the enzyme exhibited 60–68% similarity to those of other MCL-PHA depolymerases.

Keywords
Characteristics; PHO depolymerase; Pseudomonas luteola M13-4
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Characterization of an extracellular poly(3-hydroxyoctanoate) depolymerase from the marine isolate, Pseudomonasluteola M13-4
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 38, Issues 3–4, 1 February 2006, Pages 529–535
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us