ISSN: 0973-7510

E-ISSN: 2581-690X

Shuang-Hong You1, Yong-Mei He3, Bo Zhu2, Bo Wang2, Da-Wei Li3, Ri-He Peng2 and Quan-Hong Yao2
1College of Horticulture, Nanjing Agricultural University, Nanjing 210095, China.
2Shanghai Key Laboratory of Agricultural Genetics and Breeding, Agro-Biotechnology Research Institute, Shanghai Academy of Agricultural Sciences, 2901 Beidi Rd, Shanghai 201106, People’s Republic of China.
3College of Food Science, Shanghai Ocean University, Shanghai 201306, China.
J. Pure Appl. Microbiol., 2016, 10 (1): 01-10
© The Author(s). 2016
Received: 15/05/2015 | Accepted: 10/06/2015 | Published: 31/03/2016
Abstract

In this study, we analyzed the physicochemical characteristics and the structure of one glucanase and hoped it will be useful for future studies on the possible synergistic action of cellulases and it will provide guidance for the industrial utilization. A recombinant glucanase gene (r-ScEG12) from Stachybotrys chartarum was synthesized and expressed in Pichia pastoris, then was purified and characterized. The r-ScEG12 belongs to glycosyl hydrolase family 12 (GH12) by phylogenetic analysis. The Asp100, Glu117, and Glu201 residues were proposed to be present at the active site. The apparent molecular weight of r-ScEG12 was approximate 27 kDa, and the optimum temperature and pH was 40°C and 5.0, respectively. The Km and Vmax for CMC were 26.08 g/L, and 1.88 mg L-1min-1, respectively. The r-ScEG12 activity was inhibited 71.64 % and 50.97% by Cu2+ and Mn2+ respectively, while the r-ScEG12 activity was enhanced by Na+ and Ca2+ mildly.

Keywords

Endo-β-1,4-glucanase;  Biochemical characterization; Structural Modeling; Pichia pastoris;  Stachybotrys chartarum.

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© The Author(s) 2016. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License which permits unrestricted use, sharing, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.