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Heteropolysaccharide formation by Arthrobacter viscosus grown on xylose and xylose oligosaccharides

Article Abstract:

Arthrobacter viscosus NRRL B-1973 is capable of forming extracellular polysaccharides containing glucose, galactose and mannuronic acid in equal proportions from hexoses. An investigation was conducted to compare the glucose- and xylose-derived polysaccharides in terms of yield, degree of substitution and rheological characterizations. The resultsshowed that the glucose- and xylose-derived polysaccharides differed in degreesof acylation, molecular masses and intrinsic viscosities on growth in differentcarbon sources.

Author: Novak, John S., Tanenbaum, S.W., Nakas, J.P.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
Microbial metabolism, Microbial polysaccharides, Glucose metabolism

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Cloning and partial characterization of endopolygalacturonase genes from Botrytis cinerea

Article Abstract:

The cloning and partial characterization of endopolygalactorunase genes from the plant-pathogenic fungus Botrytis cinerea are described. Five monophyletic groups of homologous proteins have been identified from phylogenetic analysis of the fungus. In addition, the identity at the amino acid level between the six endopolygalacturonase genes was found to differ from 34% to 73%. Other strains of Botrytis cinerea and related species also revealed the complete endopolygalacturonase gene family.

Author: Visser, J., Mulder, W., Wubben, J.P., Have, A. Ten, Kan, J.A.L. van
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Genetic engineering, Cloning, Bacteria, Phytopathogenic, Phytopathogenic bacteria, Fungi, Pathogenic, Pathogenic fungi

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Production and characterization of laccase from Botrytis cinerea 61-34

Article Abstract:

A facile operational sequence, which includes hydrophobic interaction chromatography as the last step, helps purify extracellular laccase from Botrytis cinerea 61-34. Analysis of the enzyme reveals it as a monomeric glycoprotein containing 49% hexose. The enzyme exhibits optimum activity at 3.5 pH and 60 degrees Celsius. The stability and broad substrate range of these enzymes are favorable for commercial biotechnology transfers.

Author: Tanenbaum, S.W., Nakas, J.P., Slomczynski, D.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
Analysis, Microbial enzymes

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Subjects list: Research, Botrytis
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