Affiliation:
1. Division of Biological Sciences, National Research Council, Ottawa, Ontario, Canada K1A 0R6
Abstract
Acetivibrio cellulolyticus
cellulase obtained by the water elution of residual cellulose from the growth medium was compared with the cellulase activity present in culture supernatants. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis indicated that water elution released most of the protein bands which adhered to undigested cellulose from the culture medium. The enzyme in the culture supernatant and that eluted from residual cellulose had specific activities for Avicel hydrolysis that were 20- to 40-fold greater than that of
Trichoderma reesei
cellulase. However, Ca
2+
and a reducing agent such as dithiothreitol were required for maximum Avicel hydrolysis rates by these
A. cellulolyticus
enzyme preparations. The effect of these agents on
p
-nitrophenyl lactopyranoside hydrolysis suggested that they were required by an exoglucanase component. Supernatant enzyme preparations contained large amounts of carbohydrate which was separated from most of the cellulase protein by phenyl-Sepharose chromatography. Removal of this carbohydrate, which interfered with protein fractionations, allowed for an activity stain analysis of the supernatant enzyme.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Cited by
18 articles.
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