The β-glucanase can hydrolyze glucan in cereals such as barley and reduce the anti-nutritional effects of glucan in the digestive tract of monogastric animals.In order to obtain a strain with high β-glucanase production, Trichoderma reesei was mutated by atmospheric and room temperature plasma (ARTP).The mutant was verified by preliminary screening, rescreening, genetic stability, and enzymatic properties.Compared with the original strain, the β-glucanase activity of mutant ARTP-9 increased by 54.38%, reaching 43.75 U/mL, and its enzyme-producing ability was genetically stable.The optimum reaction temperature and pH of the enzyme were 50 ℃ and 6.0, respectively.The enzyme activity was stable in the temperature of 40-80 ℃, and pH of 2.5-6.5.The activity of this enzyme was enhanced by Fe2+, Mg2+ but inhibited by Fe3+, Mn2+, Zn2+, Ca2+, Cu2+.With β-glucan as substrate, the Km and Vmax values of the crude enzyme were 1.59 mg/mL and 6.99 μmol/(mg·min), respectively.The in vitro digestion viscosity treated with the mutant ARTP-9 solid fermentation enzyme preparation was the lowest, which was 2.23 mPa·s at 4 h of gastric phase, and 0.70 mg/mL of reducing sugar at 21 h of intestinal phase was 3.2 times that of blank.There was significant difference (P<0.05).Compared with the blank, the in vitro digestibility of barley flour treated by ARTP-9 solid fermentation enzyme preparation significantly increased by 9.02%, reaching 48.17%, and the difference was extremely significant (P<0.01).As shown by these results, the ARTP mutagenesis method could significantly improve the β-glucanase activity of T.reesei, which laid the foundation for its industrial production.
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