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Native Rhodothermus marinus Laminarinase/Lichenase
Native Rhodothermus marinus Laminarinase/Lichenase
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CAS No.:
62213-14-3
Sample Available:
Yes
Price valid (until):
2026-11-24
Company Type:
Manufactory
Location:
United States
Payment Terms:
TT against copy of documents,D/P
Average Lead Time:
15 days
Qualification:
Main Products:
Coenzymes,Inhibito,Enzymes,Zymogens,Substrates,Native Microorganism Creatine Amidinohydrolase
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Product Details
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Description
ProductName Native Rhodothermus marinus Laminarinase/Lichenase Cat No NATE-0376 Description β-glucanases degrade β-1,4-glucans of cellulose, xyloglucan and β-1,4-xylan. β-Glucanase represents a group of carbohydrate enzymes which break down glycosidic bonds within beta-glucan. It forms the main constituent of fungal cell walls and could be a potential structural and storage polysaccharide of marine macro-algae. It has the ability to degrade fungal cell walls and may be involved in defense mechanism of plants against pathogenic fungi. Abbr β-glucanase, Native Source Rhodothermus marinus Enzyme Commission Number EC 3.2.1.6 CAS No 62213-14-3 Structure The crystal structure of Laminarinase from Rhodothermus marinus (96% sequence identity with Bglu110 Laminarinase/Lichenase) has been determined to 1.9 Å resolution. – PDB entry 3ILN Specificity The molecule laminarin (also known as laminaran) is a storage glucan produced in brown algae through photosynthesis. The polysaccharide is made up of glucose residues withβ-1,3-linkages and β-1,6-linkages. It is a linear polysaccharide, with a β (1→3):β (1→6) ratio typically 3:1 but the ratio may vary with the source of the polysaccharide. Lichenin, also known as lichenan or moss starch, is a complex glucan occurring in certain species of lichensandconsists of repeating glucose units linked by β-1,3 and β-1,4 glycosidic bonds. It can be extracted from Cetraria islandica (Iceland moss). Scleroglucan, is formed by the fungus Sclerotium rolfsii. A chemically analogous polysaccharide, Schizophyllan (Sizofiran, Sonifilan, SPG) is a neutral extracellular polysaccharide produced by the fungus Schizophyllum commune. Schizophyllan is a β-1,3 beta-glucan with β-1,6 branching. Both polysaccharides share the chemical structure of the backbone with curdlan. Unit Definition One unit (U) of enzyme activity is the amount that leads to the release of 1 μmol reducing sugars per minute. Optimum pH the enzyme has optimum activity around pH 7 Optimum temperature the enzyme has optimum activity around 80°C Thermal stability The ß-galactosidase heat stability at 70,80 and 91°C Synonyms endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3 (4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1→3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucanase; endo-β-1,3-glucanase IV; endo-1,3-β-D-glucanase; 1,3-(1,3; 1,4)-β-D-glucan 3 (4)-glucanohydrolase; EC 3.2.1.6; 9074-98-0 category Feed Additive(c1431) cas_num 62213-14-3 ECHEMI Editorial ReferenceThis product has been enhanced for energy efficiency and waste prevention when used in cellulosic ethanol research.Basic Info-
Product Name:
β-Glucanase
Other Name:1,3-[1,3;1,4]-β-D-Glucan 3(4)-glucanohydrolase;β-Glucanase 2, thermostable;β-Glucanase 1, thermostable;laminarinase from trichoderma species;Glucanase, endo-1,3(4)-beta-;LAMINARINASE FROM TRICHODERMA SP. .LYOPHILIZED POWDER;Funcelase(R) from Trichoderma viride, ca. 15 U/mg
CAS No.:62213-14-3
Molecular Weight:0
EC Number:263-462-4
TSCA:TSCA listed
Color/Form:light yellow-brown
Categories:
Characteristics-
Density:
1.37[at 20℃]
Water Solubility:125g/L at 25℃
Vapor Pressure:0-0.004Pa at 25℃
Flammability characteristics:Not classified
Critical Temperature & Pressure:2-8°C
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Seller Information
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Business Type:
Manufactory
-
Main Products:
Coenzymes,Inhibito,Enzymes,Zymogens,Substrates,Native Microorganism Creatine Amidinohydrolase
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Location:
Shirley, New York 11967, USA
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Payment Terms:
TT against copy of documents,D/P
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Average lead Time:
15 days
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Total Annual Revenue:
$1 million-$2.5 million
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Year of Establishment:
2004
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