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Merck
모든 사진(1)

문서

52583

Sigma-Aldrich

Lipase B Candida antarctica immobilized on Immobead 150, recombinant from yeast

≥2000 U/g

동의어(들):

Candida antarctica Lipase

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About This Item

UNSPSC 코드:
12352204
NACRES:
NA.54

재조합

expressed in yeast

형태

beads

특이 활성도

≥2000 U/g

분자량

33 kDa

저장 온도

2-8°C

일반 설명

Lipase B or triacylglycerol ester hydrolases belongs to the class of hydrolases. Lipase B from Candida antarctica (CALB) possesses 317 amino acids and a molecular weight of 33 kDa. CALB has a catalytic triad and an open solvent accessible active site. The catalytic triad is usually Ser-His-Asp/Glu which is found in the carboxy terminal of parallel β sheet.

애플리케이션

Lipase B Candida antarctica immobilized on Immobead 150, recombinant from yeast has been used:
  • in esterification reaction of lauric acid with n-butanol in a biphasic solvent system
  • in hydrolysis of fish oil triglycerides
  • in screening of enzymes for Morita–Baylis–Hillman (MBH) reaction

Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

생화학적/생리학적 작용

Lipases B from Candida antarctica (CALB) is a versatile catalyst for biotransformation reactions. In aqueous media, CALB behaves like an esterase rather than a lipase.
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
Lipase B from Candida antarctica has been shown to be an effective catalyst for the synthesis of esters of ethyl D-glucopyranoside from fatty acids larger than octanoic acid. It has also been found to catalyze a wide variety of organic reactions including many different regio- and enantio-selective syntheses.

단위 정의

1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 7.5 and 40°C (tributyrin, Cat. No. 91010, as substrate)

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


시험 성적서(COA)

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문서 라이브러리 방문

Kinetics of acyl transfer reactions in organic media catalysed by Candida antarctica lipase B
Martinelle M and Hult K
Biochimica et Biophysica Acta, Protein Structure and Molecular Enzymology, 1251(2), 191-197 (1995)
The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
Uppenberg J, et al.
Structure, 2(4), 293-308 (1994)
Asymmetric Morita-Baylis-Hillman reaction catalyzed by pepsin
Xue JW, et al.
Journal of Molecular Catalysis. B, Enzymatic, 124, 62-69 (2016)
Thermodynamic study of hydrolysis and esterification reactions with immobilized lipases
Sharma A, et al.
European International Journal of Science and Technology, 4, 128-136 (2015)
Fatty Acid Specificity in Lipase-Catalyzed Synthesis of Glucoside Esters
O. Kirk et al.
Biocatalysis and Biotransformation, 6, 127-134 (1992)

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