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Title 

Characterization of a novel manganese dependent endoglucanase belongs in GH family 5 from Phanerochaete chrysosporium

Authors 

N D HuyC L NguyenH S ParkN H LocM S ChoiD H KimJeong-Woo SeoS M Park

Publisher 

Elsevier

Issue Date 

2016

Citation 

Journal of Bioscience and Bioengineering, vol. 121, no. 2, pp. 154-159

Keywords 

Barley strawEndoglucanaseManganese dependent enzymePhanerochaete chrysosporiumSaccharification

Abstract 

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 4.5-6.0, and 50°C-60°C, respectively. Moreover, rPcEg5A exhibited maximal activity in the pH range of 3.0-8.0, 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 β-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.

ISSN 

1389-1723

Link 

http://dx.doi.org/10.1016/j.jbiosc.2015.06.009

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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