Enzymes of carbohydrate metabolism of mycelial fungi from marine environments. beta-1,3-glucanase of the marine fungus Chaetomium indicum

Citation
Yv. Burtseva et al., Enzymes of carbohydrate metabolism of mycelial fungi from marine environments. beta-1,3-glucanase of the marine fungus Chaetomium indicum, BIOCHEM-MOS, 65(10), 2000, pp. 1175-1183
Citations number
20
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMISTRY-MOSCOW
ISSN journal
00062979 → ACNP
Volume
65
Issue
10
Year of publication
2000
Pages
1175 - 1183
Database
ISI
SICI code
0006-2979(200010)65:10<1175:EOCMOM>2.0.ZU;2-M
Abstract
Thirty samples of fungi belonging to 17 species living in marine environmen ts were studied for their ability to produce extracellular enzymes. In the culture fluids, a variety of glycosidases (beta -glucosidases, N-acetyl-bet a -glucosaminidase, beta -galactosidases, and alpha -mannosidases) and gluc anases (amylases and beta -1,3-glucanases) were found. Several cultures wer e found that could be used as efficient producers of either individual enzy mes or a whole complement of enzymes degrading carbohydrate-containing comp ounds. Optimal growth conditions for the fungus Chaetomium indicum and beta -1,S-glucanase biosynthesis were developed. beta -1,3-Glucanase was isolat ed by a combination of ion-exchange chromatography, ultrafiltration, and ge l chromatography. The molecular mass of the enzyme determined by gel-filtra tion was 54 kD. The enzyme was stable at temperatures below 50 degreesC, ha d a temperature optimum for activity at 60 degreesC, and retained activity between pH 4.5 and 7.5. The pH dependence of the beta -1,3-glucanase activi ty showed two maxima, at pH 4.4 and 5.6; this suggested the existence of tw o forms of the enzyme. Analysis of the products of enzymatic hydrolysis of laminaran, transglycosylating ability, and the effect of a specific natural inhibitor indicates that both forms are exo-beta -1,3-glucanases.