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Merck
모든 사진(1)

주요 문서

41658

Sigma-Aldrich

Lipase A Candida antarctica immobilized on Immobead 150, recombinant from Aspergillus oryzae

≥500 U/g

동의어(들):

Candida antarctica Lipase

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About This Item

UNSPSC 코드:
12352204
NACRES:
NA.54

재조합

expressed in Aspergillus oryzae

Quality Level

양식

beads (powder like)
beads

특이 활성도

≥500 U/g

저장 온도

2-8°C

관련 카테고리

일반 설명

Research area: Cellsignalling. Lipase A Candida Antarctica, CalA is a thermostable, calcium-dependent enzyme with high substrate specificity. CalA comprises of the catalytic triad (Ser184, Asp334, His366) and has an α/β hydrolase structural fold.

애플리케이션

Lipase A Candida antarctica immobilized on Immobead 150, recombinant from Aspergillus oryzae has been used in the synthesis of enantiopure (R)-salsolinol and adsorption kinetics studies using Quartz crystal microbalance with dissipation (QCM-D).It has also been used tostudy the esterification of difluorinated alcohols.
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

생화학적/생리학적 작용

Lipase A Candida Antarctica, CalA is highly specific for alcohols and esterifies the trans-isomer of fatty acids. CalA recognizes highly branched acyl groups and is active on alcohols with steric hindrance. CalA catalyzes the production of enantiopure amino acids and aids in the synthesis of chiral cyanohydrins. It may find industrial applications for its thermostable functionality in paper industry.Lipase A Candida antarctica(CAL-A) shows acetyltransferase activity by synthesizing fatty acid esters from certain alcohols and natural oils in an aqueous environment.

단위 정의

1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 10.0 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)


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문서 라이브러리 방문

Improved acylation of phytosterols catalyzed by Candida antarctica lipase A with superior catalytic activity
Panpipat W, et al.
Biochemical Engineering Journal, 70(1), 55-62 (2013)
Lipase-catalyzed synthesis of the chiral tetrahydroisoquinoline (R)-salsolinol
Ding W, et al.
Tetrahedron, 23(18-19), 1376-1379 (2012)
Orientating lipase molecules through surface chemical control for enhanced activity: a QCM-D and ToF-SIMS investigation
Joyce P, et al.
Colloids and Surfaces. B, Biointerfaces, 142, 173-181 (2016)
High yield expression of Lipase A from Candida antarctica in the methylotrophic yeast Pichia pastoris and its purification and characterisation
Pfeffer J, et al.
Applied Microbiology and Biotechnology, 72(5), 931-931 (2006)
Biotechnological applications of Candida antarctica lipase A: State-of-the-art
de Maria PD, et al.
Journal of Molecular Catalysis. B, Enzymatic, 37(1-6), 36-46 (2005)

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