추천 제품
생물학적 소스
Aspergillus sp. (Aspergillus oryzae)
Quality Level
형태
solution
특이 활성도
≥100,000 U/g
저장 조건
(Tightly closed. Dry)
기술
cell based assay: suitable
색상
beige
white
저장 온도
2-8°C
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-;
InChI key
QWZUIMCIEOCSJF-CHHCPSLASA-N
유사한 제품을 찾으십니까? 방문 제품 비교 안내
일반 설명
Research area: Cell Signaling
Lipase is derived from Aspergillus oryzae by ammonium sulfate precipitation and chromatography.Lipases or triacylglycerol acyl hydrolases are a group of hydrolase enzymes that are usually found in humans and animals with monogastric stomachs. Lipase enzymes are generally formed in the pancreas and stomach where they aid in fat and lipids digestion.(2)
Lipase is derived from Aspergillus oryzae by ammonium sulfate precipitation and chromatography.Lipases or triacylglycerol acyl hydrolases are a group of hydrolase enzymes that are usually found in humans and animals with monogastric stomachs. Lipase enzymes are generally formed in the pancreas and stomach where they aid in fat and lipids digestion.(2)
애플리케이션
Lipase from Aspergillus oryzae has been used:
- as a control enzyme in activity assays
- as a component in lipolase stock solution for the hydrolysis experiments
- to incubate scaffolds for lipase-accelerated degradation experiments
- as the lipolytic enzyme standard to detect lipolytic enzymatic activity via chromogenic agar plates and zymography
생화학적/생리학적 작용
Lipase is widely used in several industries including food and pharmaceuticals. It mediates the hydrolysis of fats and oil. Lipase is utilized for peptide synthesis and in the detergent industry. It is active in the range of pH 2-5 and temperature between 30-50°C. Metal ions such as Fe2+, Fe3+, and Cu2+ prevent the action of lipase. A less polar organic solvent is preferred for high stability.Lipases play a crucial role in digestion as well as the transportation and processing of dietary lipid substrates by catalyzing the hydrolysis of ester bonds in lipid substrates. The lipase from Aspergillus oryzae (AOL), a multipurpose biocatalyst can be used in the kinetic resolution of a biotin intermediate lactone,α-lipoic acid, and 1-phenylethanol. Additionally, it has the ability to stereoselectively catalyze the hydrolysis of ethyl 2-(4-hydroxyphenoxy) propanoate and its analogs, which are key intermediates in the production of aryloxyphenoxypropionate herbicides. AOL serves as a promising biocatalyst in the esterification of a series of short-chain acids and alcohols to produce flavor esters. It can be used to catalyze the esterification of lauric acid with aromatic alcohol-benzyl alcohol.
제조 메모
Produced by submerged fermentation of a genetically modified Aspergillus oryzae microorganism
법적 정보
A product of Novozyme Corp.
관련 제품
제품 번호
설명
가격
기질
항체
제품 번호
설명
가격
효소
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)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
Acta biomaterialia, 92, 48-59 (2019-05-21)
To maintain functionality during in situ vascular regeneration, the rate of implant degradation should be closely balanced by neo-tissue formation. It is unknown, however, how the implant's functionality is affected by the degradation of the polymers it is composed of.
Microbial Enzyme in Food Biotechnology
Enzymes in Food Biotechnology, 19-28 (2019)
Acta biomaterialia, 92, 48-59 (2019-05-21)
To maintain functionality during in situ vascular regeneration, the rate of implant degradation should be closely balanced by neo-tissue formation. It is unknown, however, how the implant's functionality is affected by the degradation of the polymers it is composed of.
Lipolase catalyzed synthesis of benzyl esters of fatty acids
Biochemical Engineering Journal, 12, 131-141 (2002)
Three-phase slug flow in microchips can provide beneficial reaction conditions for enzyme liquid-liquid reactions
Biomicrofluidics, 7(5), 054103-054103 (2013)
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