Abstract
Cellulose is the most abundant renewable resource in nature and can be used for the production of soluble sugars, biofuels and as raw materials for other important chemical products. Therefore, the development and research of multifunction’s enzyme is of great significance for the degradation and utilization of cellulose. In this study, two-step DEAE-Sepharose FF weak anion exchange of fermentation supernatant of Bacillus subtilis LC-9 with different pH buffer as mobile phase was used to obtain the electrophoretic ally pure protein with a molecular weight of about 32 KDa, 25 KDa. The specific activity of filter paper comprehensively characterized by enzyme was 22.68U/mg, the purification fold was 33.35 and the recovery rate was 20.52%. In this study, the purified multifunction’s enzyme not only has the activity of endoglucanase, xylanase, filter paper enzyme, exoglucanase and other cellulases, but also has the advantages of short enzyme producing time, simple purification method And other advantages, has a good prospect of industrialization.
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