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Title 

Purification and characterization of poly(3-hydroxylbutyrate) depolymerase from a fungal isolate, Emericellopsis minima W2

Authors 

Do Young KimJi Hye YunHyung Woo KimKyung Sook BaeYoung Ha Rhee

Publisher 

Microbiological Society of Korea

Issue Date 

2002

Citation 

Journal of Microbiology, vol. 40, no. 2, pp. 129-133

Keywords 

emericellopsis minimaPHB depolymerasepoly(3-hydroxyalkanoate)poly(3-hydroxybutyrate)3 hydroxybutyric acid4 nitrophenylacetic acid4 nitrophenylbutyrateacetic acid derivativebutyric acid derivativefungal enzyme

Abstract 

The fungus, Emericellopsis minima W2, capable of degrading poly(3-hydroxybutyrate) (PHB) was isolated from a waste water sample. Production of the PHB depolymerase from E. minima W2 (PhaZEmi) was significantly repressed in the presence of glucose. PhaZEmi was purified by column chromatography on Octyl-Sepharose CL-4B and Sephadex G-100. The molecular mass of the PhaZEmi, which consisted of a single polypeptide chain, was estimated to be 48.0 kDa by SDS-PAGE and its pI value was 4.4. The maximum activity of the PhaZEmi was observed at pH 9.0 and 55°C. It was significantly inactivated by 1 mM dithiothreitol, 2 mM diisopropyl fluorophosphate, 0.1 mM Tween 80, and 0.1 mM Triton X-100, but insensitive to phenylmethylsulfonyl fluoride and N-ethylmaleimide. The PhaZEmi efficiently hydrolyzed PHB and its copolyester with 30 mol% 3-hydroxyvalerate, but did not act on poly(3-hydroxyoctanoate). It also hydrolyzed p-nitrophenylacetate and p-nitrophenylbutyrate but hardly affected the longer-chain forms. The main hydrolysis product of PHB was identified as a dimer of 3-hydroxybutyrate.

ISSN 

1225-8873

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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