62287
南极假丝酵母脂肪酶A，重组 来源于米曲霉
powder, beige, ~2 U/mg
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.26
EC Number:
232-619-9
MDL number:
Specific activity:
~2 U/mg
Recombinant:
expressed in Aspergillus oryzae
产品名称
南极假丝酵母脂肪酶A，重组 来源于米曲霉, powder, beige, ~2 U/mg
InChI key
QWZUIMCIEOCSJF-CHHCPSLASA-N
InChI
1S/C11H9N3O2.Na/c15-8-4-5-9(10(16)7-8)13-14-11-3-1-2-6-12-11;/h1-7,16H,(H,12,14);/q;+1/b13-9-;
recombinant
expressed in Aspergillus oryzae
form
powder
specific activity
~2 U/mg
shelf life
limited shelf life, expiry date on the label
color
beige
storage temp.
2-8°C
Quality Level
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Application
南极假丝酵母脂肪酶A（米曲霉生产的重组蛋白）已用于酶催化的3-乙酰硫己醛水解研究。还用作生物催化剂，检测其对植物固醇和羊脂酸的酯化反应的影响。
Biochem/physiol Actions
南极假丝酵母脂肪酶 A 催化叔醇水解形成甘油和脂肪酸，并显示出对 β-氨基酯的 N-酰化的选择性。
南极假丝酵母脂肪酶A(CALA)是热稳定性丝氨酸水解酶，倾向于催化甘油三酯sn-2位的酯键断裂。对大分子底物和大位阻叔醇具有优异的活性。
General description
南极假丝酵母脂肪酶A(CALA)属于α/β水解酶家族。由Ser184、His366和Asp334残基组成催化三联体。
Other Notes
1个酶活性单位相当于在pH 8.0和40°C条件下，每分钟水解1 μmol油酸所需的酶量（使用甘油三油酸酯作为底物，货号62314）。如上所述，1个酶活性单位相当于在pH 8.0和70°C条件下，使用甘油三丁酸酯作为底物时的约0.15个酶活性单位
特性
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
常规特殊物品
此项目有
S.A. Patkar et al.
Indian Journal of Chemistry, 76-76 (1993)
Integrated enzymatic production of specific structured lipid and phytosterol ester compositions
Hellner G, et al.
Process. Biochem., 45(8), 1245-1250 (2010)
Biotechnological relevance of the lipase A from Candida antarctica
Monteiro RRC, et al.
Catalysis Today, 362, 141-154 (2021)
Anders G Sandström et al.
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
Hidehiko Wakabayashi et al.
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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