Heterologous expression and biochemical characterization of a thermostable endo-β-1,4-glucanase from Colletotrichum orchidophilum View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2020-08-09

AUTHORS

Hai-Yan Zhou, Jian-Bao Zhou, Xiao-Nan Yi, Yan-Mei Wang, Ya-Ping Xue, De-Shui Chen, Xin-Ping Cheng, Mian Li, Hong-Yan Wang, Kai-Qian Chen, Zhi-Qiang Liu, Yu-Guo Zheng

ABSTRACT

To develop new cellulases for efficient utilization of the lignocellulose, an endoglucanase (CoCel5A) gene from Colletotrichum orchidophilum was synthesized and a recombinant Pichia pastoris GS115/pPIC9K/cocel5A was constructed for secretory expression of CoCel5A. After purification, the protein CoCel5A was biochemically characterized. The endoglucanase CoCel5A exhibited the optimal activity at 55–75 °C and high thermostability (about 85% residual activity) at the temperature of 55 °C after incubation for 3 h. The highest activity of CoCel5A was detected when 100 mM citric acid buffer (pH 4.0–5.0) was used and excellent pH stability (up to 95% residual activity) was observed after incubation in 100 mM citric acid buffer (pH 3.0–6.0) at 4 °C for 24 h. Carboxymethyl cellulose sodium salt (n = approx. 500) (CMC) and β-d-glucan were the best substrates for CoCel5A among the tested substrates. The kinetic parameters Vmax, Km, and Kcat/Km values against CMC were 290.70 U/mg, 2.65 mg/mL, and 75.67 mL/mg/s, respectively; and 228.31 U/mg, 2.06 mg/mL, and 76.45 mL/mg/s against β-d-glucan, respectively, suggesting that CoCel5A has high affinity and catalytic efficiency. These properties supported the potential application of CoCel5A in biotechnological and environmental fields. More... »

PAGES

67-79

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00449-020-02420-7

DOI

http://dx.doi.org/10.1007/s00449-020-02420-7

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1130001386

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/32772153


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25 schema:description To develop new cellulases for efficient utilization of the lignocellulose, an endoglucanase (CoCel5A) gene from Colletotrichum orchidophilum was synthesized and a recombinant Pichia pastoris GS115/pPIC9K/cocel5A was constructed for secretory expression of CoCel5A. After purification, the protein CoCel5A was biochemically characterized. The endoglucanase CoCel5A exhibited the optimal activity at 55–75 °C and high thermostability (about 85% residual activity) at the temperature of 55 °C after incubation for 3 h. The highest activity of CoCel5A was detected when 100 mM citric acid buffer (pH 4.0–5.0) was used and excellent pH stability (up to 95% residual activity) was observed after incubation in 100 mM citric acid buffer (pH 3.0–6.0) at 4 °C for 24 h. Carboxymethyl cellulose sodium salt (n = approx. 500) (CMC) and β-d-glucan were the best substrates for CoCel5A among the tested substrates. The kinetic parameters Vmax, Km, and Kcat/Km values against CMC were 290.70 U/mg, 2.65 mg/mL, and 75.67 mL/mg/s, respectively; and 228.31 U/mg, 2.06 mg/mL, and 76.45 mL/mg/s against β-d-glucan, respectively, suggesting that CoCel5A has high affinity and catalytic efficiency. These properties supported the potential application of CoCel5A in biotechnological and environmental fields.
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32 schema:keywords CMC
33 CoCel5A
34 CoCel5A.
35 Colletotrichum orchidophilum
36 GS115/pPIC9K/cocel5A
37 Km
38 Km values
39 Pichia pastoris GS115/pPIC9K/cocel5A
40 Vmax
41 acid buffer
42 activity
43 affinity
44 applications
45 biochemical characterization
46 buffer
47 carboxymethyl
48 catalytic efficiency
49 cellulases
50 characterization
51 citric acid buffer
52 efficiency
53 efficient utilization
54 endo
55 endoglucanase CoCel5A
56 endoglucanase gene
57 environmental fields
58 excellent pH stability
59 expression
60 field
61 genes
62 glucan
63 glucanase
64 good substrate
65 heterologous expression
66 high activity
67 high affinity
68 high thermostability
69 incubation
70 kcat/Km values
71 kinetic parameters Vmax
72 lignocellulose
73 mM citric acid buffer
74 new cellulases
75 optimal activity
76 orchidophilum
77 pH stability
78 pPIC9K/cocel5A
79 parameters Vmax
80 pastoris GS115/pPIC9K/cocel5A
81 potential applications
82 properties
83 protein CoCel5A
84 purification
85 recombinant Pichia pastoris GS115/pPIC9K/cocel5A
86 salt
87 secretory expression
88 sodium salt
89 stability
90 substrate
91 temperature
92 thermostability
93 thermostable endo
94 utilization
95 values
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