Expression of a secretory β-glucosidase from Trichoderma reesei in Pichia pastoris and its characterization

2011 ◽  
Vol 33 (12) ◽  
pp. 2475-2479 ◽  
Author(s):  
Ping Chen ◽  
Xianyu Fu ◽  
Tzi Bun Ng ◽  
Xiu-Yun Ye
Keyword(s):  
Pichia Pastoris ◽  
Trichoderma Reesei

Heterologous expression of codon optimized Trichoderma reesei Cel6A in Pichia pastoris

2016 ◽  
Vol 92 ◽  
pp. 107-116 ◽  
Author(s):  
Fubao Fuelbiol Sun ◽  
Renhui Bai ◽  
Huimin Yang ◽  
Fei Wang ◽  
Jing He ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Heterologous Expression ◽  
Trichoderma Reesei

From in silico to in vitro: Modelling and production of Trichoderma reesei endoglucanase 1 and its mutant in Pichia pastoris

2012 ◽  
Vol 159 (1-2) ◽  
pp. 61-68 ◽  
Author(s):  
Gunseli Bayram Akcapinar ◽  
Ozgur Gul ◽  
Ugur O. Sezerman
Keyword(s):  
Pichia Pastoris ◽  
Trichoderma Reesei ◽  
In Silico ◽  
In Vitro Modelling

Effect of codon optimization on the expression of Trichoderma reesei endoglucanase 1 in Pichia pastoris

2011 ◽  
Vol 27 (5) ◽  
pp. 1257-1263 ◽  
Author(s):  
Gunseli Bayram Akcapinar ◽  
Ozgur Gul ◽  
Ugur Sezerman
Keyword(s):  
Pichia Pastoris ◽  
Trichoderma Reesei ◽  
Codon Optimization

scholarly journals Expression and characterization of Trichoderma reesei endoglucanase II in Pichia pastoris under the regulation of the GAP promoter

2020 ◽  
Vol 25 (2) ◽  
pp. 127
Author(s):  
Kezia Abib Yerah Tjandra ◽  
Kartika Sari Dewi ◽  
Asrul Muhamad Fuad ◽  
Trisanti Anindyawati
Keyword(s):  
Pichia Pastoris ◽  
Trichoderma Reesei ◽  
Specific Activity ◽  
Catalytic Efficiency ◽  
Endoglucanase Activity ◽  
Gap Promoter ◽  
Sds Page ◽  
Optimum Ph ◽  
High Concentrations

Trichoderma reesei is known to be one of the organisms capable for producing various types of cellulase in high concentrations. Among these cellulases, the highest catalytic efficiency of endoglucanases II (EGII, EC 3.2.1.4) are considered important for industrial application. The characterization of the EGII is necessary since it is widely used in high-temperature reactions in the industries. In this study, the recombinant EGII protein was expressed in Pichia pastoris and it has a molecular mass of approximately 52 kDa. Recombinant EGII was purified using Ni-NTA affinity chromatography and characterized by SDS-PAGE and western blot analyses. The enzyme activity of recombinant EGII was measured using the Nelson Somogyi method to determine its optimum pH and temperature. The result showed that the maximum EGII expression was achieved after 72 h of culture incubation. The crude enzyme has optimum activity at pH 5.0, resulting in 16.3 U/mL and 14.6 U/mL activity at 40 °C and 50 °C, respectively. While the purified enzyme gave the specific activity of 115.7 U/mg under the optimum condition. Finally, our study demonstrated that recombinant EGII could retain the endoglucanase activity for 89% and 80% at 40 °C and 50 °C, respectively.

scholarly journals Use of HDEL-tagged Trichoderma reesei mannosyl oligosaccharide 1,2-α-D -mannosidase for N -glycan engineering in Pichia pastoris

FEBS Letters ◽  
2001 ◽  
Vol 503 (2-3) ◽  
pp. 173-178 ◽  
Author(s):  
Nico Callewaert ◽  
Wouter Laroy ◽  
Hasan Cadirgi ◽  
Steven Geysens ◽  
Xavier Saelens ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Trichoderma Reesei

Cloning and Expression of Trichoderma reesei Cellobiohydrolase I in Pichia pastoris

1999 ◽  
Vol 15 (5) ◽  
pp. 828-833 ◽  
Author(s):  
S. Godbole ◽  
S.R. Decker ◽  
R.A. Nieves ◽  
W.S. Adney ◽  
T.B. Vinzant ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Trichoderma Reesei ◽  
Cloning And Expression ◽  
Cellobiohydrolase I
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