Characterization of a novel manganese dependent endoglucanase belongs in GH family 5 from Phanerochaete chrysosporium
Summary: The cDNA encoding a putative glycoside hydrolase family 5, which has been predicted to be an endoglucanase (PcEg5A), was cloned from Phanerochaete chrysosporium and expressed in Pichia pastoris. PcEg5A contains a carbohydrate-binding domain and two important amino acids, E209 and E319, playing as proton donor and nucleophile in substrate catalytic domain. SDS-PAGE analysis indicated that the recombinant endoglucanase 5A (rPcEg5A) has a molecular size of 43 kDa which corresponds with the theoretical calculation. Optimum pH and temperature were found to be 4.5e6.0, and 50 Ce60 C, respectively. Moreover, rPcEg5A exhibited maximal activity in the pH range of 3.0e8.0, whereas over 50% of activity still remained at 20 C and 80 C. rPcEg5A was stable at 60 C for 12 h incubation, indicating that rPcEg5A is a thermostable enzyme. Manganese ion enhanced the enzyme activity by 77%, indicating that rPcEg5A is a metal dependent enzyme. The addition of rPcEg5A to cellobiase (cellobiohydrolase and b-glucosidase) resulted in a 53% increasing saccharification of NaOH-pretreated barley straw, whereas the glucose release was 47% higher than that cellobiase treatment alone. Our study suggested that rPcEg5A is an enzyme with great potential for biomass saccharification.
Type: SCOPUS listed journals
Author: Nguyễn Đức Huy, Cu Le Nguyen, Han-Sung Park, Nguyễn Hoàng Lộc, Myoung-Suk Choi, Dae-Hyuk Kim, Jeong-Woo Seo, Seung-Moon Park
Unit: Director board of Institute
Journal:Journal of Bioscience and Bioengineering
Issue, Number, Pages1-6
ISSN/ISBN:1389-1723, E - ISSN: 1347 - 4421
Impact factor:2.240
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Year of publication: 2016
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