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 enzyme, LicA. The temperature at which 50% inactivation occurred after heat treatment for 10 min was increased by 14 degrees C for 2011D, in comparison to those of wild-type enzyme.
Kim
Suk-Am
SA
Institute of BioAgricultural Sciences, Academia Sinica, Taipei, Taiwan, Republic of China.
Cheng
Kuo-Joan
KJ
Liu
Jin-Hao
JH
D019943:Amino Acid Substitution; D004795:Enzyme Stability; D014644:Genetic Variation; D006026:Glycoside Hydrolases / Q000235:genetics* / Q000378:metabolism; D006361:Heating; D016296:Mutagenesis; D020085:Neocallimastigales / Q000201:enzymology* / Q000235:genetics
D006026:Glycoside Hydrolases; C028020:licheninase