Affiliation:
1. Unité de Génétique, Université Catholique de Louvain, Place Croix du Sud 4 (bte 3), B-1348 Louvain-la-Neuve, Belgium
Abstract
Several enzymatic properties of an endoglucanase produced in
Escherichia coli
by a gene from
Pseudomonas fluorescens
subsp.
cellulosa
were investigated. Gel filtration revealed a single peak of
M
r
36,000 with endoglucanase activity. The pH optimum of the enzyme was 7.0. Carboxymethyl cellulose and barley β-glucan (mixed β-1,3 and 1,4 linkages) were good substrates, but not laminarin (β-1,3 linkages), amylose, filter paper, microcrystalline cellulose (Avicel), or cellotriose. The mode of action was typical of an “endo”-acting enzyme. Taken together, these properties do not correspond to those of any of the endoglucanases described in
P. fluorescens
subsp.
cellulosa
. Consequently, the gene was designated
egIX
. The enzyme was sensitive to end-product inhibition by cellobiose but was only moderately inhibited by glucose. The enzyme was formed constitutively in
E. coli
throughout the growth phase. Urea had no effect on endoglucanase synthesis, but glucose acted as a catabolite repressor. The formation of the enzyme in
E. coli
was partially dependent on cyclic AMP.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Cited by
10 articles.
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