추천 제품
일반 설명
Lipase A Candida antarctica (CALA) belongs to the α/β hydrolase family. The catalytic triad comprises Ser184, His366, and Asp334 residues.
애플리케이션
Lipase A Candida antarctica, recombinant from Aspergillus oryzae has been used in the enzyme-catalyzed hydrolysis studies with 3-acetylthiohexanal. It has also been used as a biocatalyst to test its effect on the esterification of phytosterol with caprylic acid.
생화학적/생리학적 작용
Lipase A Candida antarctica (CALA) is a thermostable serine hydrolase with a higher sn-2 preference towards triglycerides. It displays excellent activity towards large substrates as well as bulky sterically hindered tertiary alcohols.
Lipase A from Candida Antarctica catalyzes hydrolysis of tertiary alcohols to form glycerol and fatty acids and shows selectivity for the N-acylation of β-amino esters.
단위 정의
1 U corresponds to the amount of enzyme which liberates 1 μmol oleic acid per minute at pH 8.0 and 40°C (triolein, Cat. No. 62314, as substrate); 1 U as described above is equivalent to ~0.15 U using trybutyrine, Cat. No. 91010, as substrate, at pH 8.0 and 70°C
기타 정보
Characterization
교체됨
제품 번호
설명
가격
신호어
Danger
유해 및 위험 성명서
예방조치 성명서
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
이미 열람한 고객
Protein engineering, design & selection : PEDS, 22(7), 413-420 (2009-06-11)
We herein report the first directed evolution of Candida antarctica lipase A (CalA), employing a combinatorial active-site saturation test (CAST). Wild-type CalA has a modest E-value of 5.1 in kinetic resolution of 4-nitrophenyl 2-methylheptanoate. Enzyme variants were expressed in Pichia
Biotechnological relevance of the lipase A from Candida antarctica
Catalysis Today, 362, 141-154 (2021)
Integrated enzymatic production of specific structured lipid and phytosterol ester compositions
Process. Biochem., 45(8), 1245-1250 (2010)
Indian Journal of Chemistry, 76-76 (1993)
Journal of agricultural and food chemistry, 51(15), 4349-4355 (2003-07-10)
The enantioselectivity of the generation of 3-mercaptohexanal and 3-mercaptohexanol, two potent sulfur-containing aroma compounds, by lipase-catalyzed hydrolysis of the corresponding 3-acetylthioesters was investigated. The stereochemical course of the kinetic resolutions was followed by capillary gas chromatography using modified cyclodextrins as
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