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CMC‐liquefying enzyme, a low molecular mass initial cellulose‐decomposing cellulase responsible for fragmentation from Streptomyces sp. LX
Author(s) -
Li X.,
Gao P.
Publication year - 1997
Publication title -
journal of applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 1364-5072
DOI - 10.1046/j.1365-2672.1997.00191.x
Subject(s) - cellulase , depolymerization , enzyme , fragmentation (computing) , filter paper , cellulose , chemistry , enzyme assay , incubation , molecular mass , biochemistry , chromatography , organic chemistry , biology , ecology
Streptomyces sp. LX, newly isolated from soil, was shown to secrete a carboxylmethylcellulose (CMC)‐liquefying enzyme that cleaves the CMC chains, releasing negligible reducing terminals. The new enzyme, named component C 2 , was purified to homogeneity by dialysation. It has a molecular mass of 9·8 kDa. The pH optimum of the enzyme activity is 6·4 and its temperature optimum is 50°C. It retains full activity at pH 4–6·4 upon incubation at 50°C for 30 min. The enzyme has significant fragmentation activity on filter paper despite the absence of weight loss, release of reducing sugars and depolymerization during incubation with filter paper. The one‐electron oxidative reaction is shown not to participate in the fragmentation of filter paper by enzyme C 2 .