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Multifactional glucanases

Biotechnology Advances, 1996
Diverse functional roles of multifunctional proteins arise from either their independent functional domains or dual activities mediated through a single active site. Presence of multifunctional proteins significantly enhances the metabolic efficiency of a cell.
N N, Kumar, D N, Deobagkar
openaire   +2 more sources

Laminarans and 1,3-β-D-glucanases

International Journal of Biological Macromolecules, 2020
The laminarans are biologically active water-soluble polysaccharide (1,3;1,6-β-D-glucans) of brown algae. These polysaccharides are an attractive object for research due to its relatively simple structure, low toxicity, and various biological effects.
Roza V, Usoltseva   +5 more
openaire   +3 more sources

Glucosidases and exo-glucanases

Canadian Journal of Biochemistry, 1968
A comparison was made of exo-α-glucanases with α-glucosidases, and of exo-β1 → 3-glucanases with β-glucosidases to establish criteria for their characterization. Dimers, trimers, and tetramers of glucose are substrates for both exo-glucanases and glucosidases. Exo-glucanases act more rapidly on the longer oligomers, glucosidases on the shorter.
E T, Reese, A H, Maguire, F W, Parrish
openaire   +2 more sources

The glucanases of Cellulomonas

Biotechnology Advances, 1997
Cellulomonas is a unique bacterium possessing not only the capacity to degrade various carbohydrates, such as starch, xylan and cellulose, but crystalline cellulose as well. It has developed a complex battery of glucanases to deal with substrates possessing such extensive microheterogeneities. Some of these enzymes are multifunctional, as well as cross
P, Chaudhary, N N, Kumar, D N, Deobagkar
openaire   +2 more sources

Characterization of 1,3-β-glucanase and 1,3;1,4-β-glucanase genes from Phytophthora infestans

Fungal Genetics and Biology, 2003
Three putative exo-1,3-beta-glucanase genes (Piexo1, Piexo2, Piexo3), one endo-1,3-beta-glucanase (Piendo1) and one endo-1,3;1,4-beta-glucanase (Piendo2) gene were cloned and characterized from the oomycete Phytophthora infestans. Southern hybridization revealed that Piexo1, Piexo2, Piexo3, and Piendo2 are single copy, and that Piendo1 is encoded by ...
Adele, McLeod   +2 more
openaire   +2 more sources

YEAST GLUCANASE AND MANNANASE

Journal of the Institute of Brewing, 1971
Synchronously-dividing cultures of brewer's yeast show cyclical changes in activities of mannanase, glucanase and laminarinase, suggesting that these enzymes may have a function in the budding process. The same enzymes are present in autolysates of brewer's yeast; the laminarinase completely hydrolyses laminarin to monosaccharide but the others yield ...
I. S. Maddox, J. S. Hough
openaire   +1 more source

Proteinaceous inhibitors of endo-β-glucanases

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2004
Both plants and filamentous phytopathogens secrete proteins that inhibit endo-beta-glucanases. The first endo-beta-glucanase inhibitor proteins to be discovered are XEGIP, a tomato protein that inhibits fungal xyloglucan-specific endo-beta-1,4-glucanases, and GIP1, an oomycete protein that inhibits endo-beta-1,3-glucanases produced by the plant host ...
William S, York   +2 more
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Microbial β-Glucanases Different from Cellulases

Critical Reviews in Biotechnology, 1991
The beta-glucans different from cellulose are the most abundant class of polysaccharides. They are found in microorganisms and higher plants as structural entities of cell wall, as cytoplasmic and vacuolar reserve materials, and as extracellular substances. Enzyme systems capable to hydrolyze beta-glucans are produced by different microorganisms.
S, Bielecki, E, Galas
openaire   +2 more sources

β-D-1,6-Glucanase in Streptomyces

Nature, 1963
ACCORDING to Reese et al.1, β-D-1,6-glucan rarely occurs in Nature, yet many fungi are able to produce an enzyme capable of hydrolysing it. Production of β-D-1,6-glucanase by Streptomyces has not been reported.
N, NAKAMURA, O, TANABE
openaire   +2 more sources

Measurement of endo-1,4-β-Glucanase

2012
Several procedures are available for the measurement of endo-1,4-β-glucanase (EG). Primary methods employ defined oligosaccharides or highly purified polysaccharides and measure the rate of hydrolysis of glycosidic bonds using a reducing-sugar method. However, these primary methods are not suitable for the measurement of EG in crude fermentation broths
Barry V, McCleary   +2 more
openaire   +2 more sources

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