Characterization of the endoglucanase and glucomannanase activities of a glycoside hydrolase family 45 protein from Penicillium decumbens 114-2

The Journal of General and Applied Microbiology
Guodong LiuYinbo Qu

Abstract

The gene encoding a glycoside hydrolase (GH) family 45 endoglucanase (Cel45A) was cloned from P. decumbens 114-2 and expressed in Pichia pastoris. To our knowledge, this is the first report of characterization of a GH family 45 protein from Penicillium species. The purified recombinant enzyme showed a higher activity on konjac glucomannan (KGM) than on sodium carboxymethyl cellulose (CMC-Na) or phosphoric acid swollen cellulose (PASC). The highest hydrolytic activity was detected at pH5.0 on KGM and pH 3.5 on CMC-Na, indicating the mode of action on the two substrates may be different for Cel45A. The optimum temperatures on the two substrates were both 60 degrees C and about 90% relative activities were retained at 70 degrees C. Products released from PASC and CMC-Na were mainly cellobiose, cellotriose and cellotetraose. The protein with higher glucomannanase activity might help the efficient degradation of lignocellulose by P. decumbens in the natural state.

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Citations

Dec 8, 2011·Microbial Cell Factories·Marie CouturierJean-Guy Berrin
Aug 29, 2014·World Journal of Microbiology & Biotechnology·Bin TangXianglin Li
Oct 27, 2015·Bioprocess and Biosystems Engineering·Burcu Gündüz Ergün, Pınar Çalık
Aug 13, 2017·Biotechnology and Bioengineering·Chiara GandiniRoberto Mazzoli
Jan 30, 2015·Chemical Reviews·Christina M PayneGregg T Beckham

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