Biotechnology Letters, Vol.24, No.8, 595-601, 2002
Separation of two functional domains of the family F/10 beta-xylanase from Streptomyces olivaceoviridis E-86 limited proteolysis with papain and some of their properties
Limited proteolysis of papain on the intact family F/10 beta-xylanase (45 kDa) led to the isolation of catalytic domain (32 kDa) and xylan-binding domain (15 kDa). The two truncated protein fragments were purified by gel filtration to homogeneity. The purified catalytic domain was fully active against 4-O-methyl-d-glucurono-d-xylan, and the action mode on xylan was the same as the intact xylanase. However, the removal of xylan-binding domain reduces dramatically the capability of adsorption for xylan.