Rao, US and Murthy, SK (1988) Purification and characterization of a beta-glucosidase and endocellulase from Humicola insolens. In: Indian Journal of Biochemistry & Biophysics, 25 (6). pp. 687-694.Full text not available from this repository.
A .beta.-glucosidase and an endocellulase were purified from the culture filtrates of a thermophilic cellulolytic fungus Humicola insolens. Both the preparations were homogeneous by PAGE, ultracentrifugation and gel filtration (Mr 45,000). Ouchterlony immunodiffusion showed complete cross reactivity between the antibodies and the two enzyme antigens, indicating the presence of a common epitope on the two enzyme proteins. The two enzymes, however, differ in their amino acid composition and their substrate specificity. .beta.-Glucosidase acts on p-nitrophenyl .beta.-D-glucopyranoside and hydrolyses cellulose to release mainly glucose and small amounts of cellobiose from the non-reducing end. On the other hand, endocellulase hydrolyses cellulose to release cellopentaose, cellotetraose, cellotriose along with cellobiose and glucose and also hydrolyses larch wood xylan.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to National Institute of Science Communication and Information Resources.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||29 Sep 2010 07:51|
|Last Modified:||29 Sep 2010 11:23|
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