9001-62-1
9001-62-1
Chemical Structure
Lipase,Candida antarctica (Immobilized)
- CAS No.: 9001-62-1
- Formula:N/A
- Molecular Weight:N/A
SMILES: [Lipase,Candida antarctica (Immobilized)]
Biological Activity: Lipase,Candida antarctica (Immobilized) is an immobilized lipase isolated from Candida antarctica fraction B. Lipase,Candida antarctica (Immobilized) features high stability and selectivity. Lipase,Candida antarctica (Immobilized) is widely used in fields such as chemical synthesis, food oil modification, and biodiesel production[1][2].
| Cat. No. | Product Name | Purity | Description | Pricing | |||||||||||||||||||
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Lipase,Candida antarctica (Immobilized) | Lipase,Candida antarctica (Immobilized) is an immobilized lipase isolated from Candida antarctica fraction B. Lipase,Candida antarctica (Immobilized) features high stability and selectivity. Lipase,Candida antarctica (Immobilized) is widely used in fields such as chemical synthesis, food oil modification, and biodiesel production. | |||||||||||||||||||||
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Lipase,Aspergillusniger (Immobilized) | Lipase, Aspergillus niger (Immobilized) is an immobilized triacylglycerol acyl hydrolase and biocatalyst. Lipase, Aspergillus niger (Immobilized) broadly catalyzes the hydrolysis of glycerol-long-chain fatty acid esters, exhibits positional selectivity for the 1,3-positions of glycerol, but shows low hydrolysis efficiency for castor oil. Lipase, Aspergillus niger (Immobilized) displays optimal activity at 45°C and pH 7.0, and remains stable at temperatures up to 60°C and over a broad pH range of 2.0-9.0. Lipase, Aspergillus niger (Immobilized) is activated by Ca2+ and Mg2+, but inhibited by Mn2+, Fe2+ and Zn2+. |
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Triacylglycerol lipase | Triacylglycerol lipase is an enzyme catalyzing the hydrolysis of triacylglycerol. Triacylglycerol lipase promotes fat decomposition, providing energy and lipid precursors for cells. Triacylglycerol lipase is used in the research of metabolic diseases such as diabetes and obesity. | |||||||||||||||||||||
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Lipase,Burkholderiacepacia (Immobilized) | Lipase,Burkholderiacepacia (Immobilized) comes from Burkholderiacepacia and can be used for catalytic reaction. | |||||||||||||||||||||
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Lipase,Candida cylindracea (Immobilized) | Lipase, Candida cylindracea (Immobilized) is an immobilized hydrolase and biocatalyst with relaxed positional and substrate specificity. Lipase, Candida cylindracea (Immobilized) can target primary and secondary ester bonds to completely hydrolyze triglycerides into fatty acids and glycerol, producing only trace amounts of monoglycerides. Lipase, Candida cylindracea (Immobilized) exhibits chain specificity, with a relatively fast hydrolysis rate for oleic acid and lauric acid chains, and the slowest hydrolysis rate for stearic acid chains. Lipase, Candida cylindracea (Immobilized) shows high catalytic activity toward long-chain triglycerides under the conditions of pH 8.0 and 37°C. |
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Lipase (MS grade) | Lipase (MS grade) catalyzes the hydrolysis of triacylglycerols to release long-chain fatty acids in a site-specific manner. Lipase (MS grade) is involved in a variety of biological processes, from fat metabolism to cell signaling and inflammation, and can be used to study diseases such as pancreatic insufficiency, celiac disease and cystic fibrosis. | |||||||||||||||||||||
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Lipase,Pseudomonas fluorescens (Immobilized) | Lipase, Pseudomonas fluorescens (Immobilized) is an immobilized biocatalyst derived from Pseudomonas fluorescens. Lipase, Pseudomonas fluorescens (Immobilized) efficiently catalyzes the hydrolysis, esterification and transesterification of triacylglycerols in solvent-free systems, and is particularly suitable for biodiesel production from soybean oil and selective modification of oils rich in EPA and DHA. Lipase, Pseudomonas fluorescens (Immobilized) exhibits optimal activity at pH 8.5 and 45°C, and retains residual activity after repeated cycles of use. Lipase, Pseudomonas fluorescens (Immobilized) is activated by Ca2+, but inhibited by Co2+, Ni2+, Fe3+, Fe2+ and EDTA. |
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References
- [1]. Zhao-Yu Wang, et al. Influence of substituent groups in regioselective acylation of nucleosides by Novozym 435 lipase. Process Biochemistry. Volume 48, Issue 8, August 2013, Pages 1208-1211.
- [2]. Ortiz C, et al. Novozym 435: the “perfect” lipase immobilized biocatalyst?. Catalysis Science & Technology, 2019, 9(10): 2380-2420.
