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Lipase aus Aspergillus oryzae
lyophilized, powder, white, ~50 U/mg
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About This Item
Empfohlene Produkte
Form
powder
Qualitätsniveau
Qualität
lyophilized
Spezifische Aktivität
~50 U/mg
Farbe
white
Lagertemp.
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-;
InChIKey
QWZUIMCIEOCSJF-CHHCPSLASA-N
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Allgemeine Beschreibung
Lipase is a carboxylesterase, which belongs to the α/β hydrolase fold family. It consists of a lid domain, hinge domain, and a catalytic triad Ser-His-Asp/Glu. Aspergillus oryzae lipase has a three-dimensional structure is an α/β hydrolase fold similar to that of the esterase enzyme.
Anwendung
Lipase from Aspergillus oryzae has been used as a component of mixed enzyme solution to determine the viable cell numbers in the biofilms formed by Listeria monocytogenes strains.
Biochem./physiol. Wirkung
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids. Aspergillus oryzae lipase might be used in the production of biodiesel from waste cooking oil. It is used in the acetylation of cellulose and ochratoxin A degradation, and asymmetric organic synthesis. Lipase from Aspergillus oryzae is an industrial enzyme that has various uses in food, detergent, and pharmaceutical industries. It is useful in immobilization studies for 1,3-dioleoyl-2-palmitoylglycerol (OPO) synthesis.
Einheitendefinition
1 U entspricht der Enzymmenge, die 1 μmol Ölsäure pro Minute bei pH 8.0 und 40°C freisetzt (Triolein, Fluka®-Nr. 62314 als Substrat)
Signalwort
Danger
H-Sätze
P-Sätze
Gefahreneinstufungen
Resp. Sens. 1
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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Lipases: from production to applications
Melani N, et al.
Separation & Purification Reviews, 49(2), 143-158 (2020)
Youwen Pan et al.
Applied and environmental microbiology, 76(5), 1433-1441 (2010-01-06)
Biofilm formation by Listeria monocytogenes is generally associated with its persistence in the food-processing environment. Serotype 1/2a strains make up more than 50% of the total isolates recovered from food and the environment, while serotype 4b strains are most often
Haiying Cai et al.
PloS one, 10(7), e0133857-e0133857 (2015-07-29)
The enzymatic synthesis of 1,3-dioleoyl-2-palmitoylglycerol (OPO), one of the main components of human milk fats, has been hindered by the relatively high cost of sn-1,3-specific lipases and the deficiency in biocatalyst stability. The sn-1,3-specific lipase from Aspergillus oryzae (AOL) is
Hedwig Strohalm et al.
Journal of agricultural and food chemistry, 58(10), 6328-6333 (2010-04-27)
The preparation of ester enantiomers (acetates, butanoates, hexanoates and octanoates) of the secondary alcohols 2-pentanol, 2-heptanol and 2-nonanol via lipase-catalyzed kinetic resolutions was investigated. Conversion rates and stereochemical courses of esterification and hydrolysis reactions catalyzed by commercially available enzyme preparations
Guan-Chun Chen et al.
Biotechnology letters, 33(3), 525-529 (2010-11-04)
Triacylglycerol lipase from Pseudomonas cepacia and Fe(3)O(4) magnetic nanoparticles were encapsulated simultaneously within biomimetic silica through the catalysis of polyallylamine. The encapsulation efficiency reached 96% with an activity recovery of 51%. After 5 h at 37°C, the activities of the
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