A variant of Orpinomyces joyonii 1,3-1,4-beta-glucanase with increased thermal stability obtained by random mutagenesis and screening

A thermostable variant of an Orpinomyces joyonii beta-glucanase was identified by screening a mutant library constructed using error-prone PCR products. The mutant, designated 2011D, had one amino acid substitution (Val replaced Asp-70). 2011D showed similar catalytic efficiency to its wild-type enz...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2002-01, Vol.66 (1), p.171-174
Hauptverfasser:	Kim, S.A. (Academia Sinica, Taipei (Taiwan)), Cheng, K.J, Liu, J.H
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution BETA GLUCANASE Biological and medical sciences Biotechnology DNA DNA shuffling Enzyme Stability Fundamental and applied biological sciences. Psychology FUNGI Genetic Variation Glycoside Hydrolases - genetics Glycoside Hydrolases - metabolism HEAT TREATMENT Heating Methods. Procedures. Technologies Mutagenesis MUTAGENICITY Neocallimastigales - enzymology Neocallimastigales - genetics PCR Protein engineering random mutagensis SELECTION thermal stability VARIANTS β-glucanase
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Zusammenfassung:	A thermostable variant of an Orpinomyces joyonii beta-glucanase was identified by screening a mutant library constructed using error-prone PCR products. The mutant, designated 2011D, had one amino acid substitution (Val replaced Asp-70). 2011D showed similar catalytic efficiency to its wild-type enzyme, Lica. The temperature at which 50% inactivation occurred after heat treatment for 10 min was increased by 14degC for 2011D, in comparison to those of wild-type enzyme.
ISSN:	0916-8451 1347-6947
DOI:	10.1271/bbb.66.171