62285
Lipase from Aspergillus oryzae
lyophilized, powder, white, ~50 U/mg
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-619-9
MDL number:
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Product Name
Lipase from Aspergillus oryzae, lyophilized, powder, white, ~50 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-;
form
powder
quality
lyophilized
specific activity
~50 U/mg
color
white
storage temp.
2-8°C
Quality Level
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This Item | L0777 | 62302 | L4277 |
|---|---|---|---|
| specific activity ~50 U/mg | specific activity ≥100,000 U/g | specific activity 15-25 U/mg | specific activity ≥20,000 U/g |
| form powder | form solution | form lyophilized solid, powder (fine) | form lyophilized |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
| Quality Level 100 | Quality Level 200 | Quality Level 100 | Quality Level 200 |
| color white | color beige, white | color - | color - |
| quality lyophilized | quality - | quality lyophilized | quality - |
Application
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.[1]
Biochem/physiol Actions
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.[2]
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.[3] Aspergillus oryzae lipase might be used in the production of biodiesel from waste cooking oil.[4] It is used in the acetylation of cellulose and ochratoxin A degradation, and asymmetric organic synthesis.[5] Lipase from Aspergillus oryzae is an industrial enzyme that has various uses in food, detergent, and pharmaceutical industries.[4][5] It is useful in immobilization studies for 1,3-dioleoyl-2-palmitoylglycerol (OPO) synthesis.[6]
General description
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.[5]
Other Notes
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)
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
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
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
Zhengyu Shu et al.
Biotechnology progress, 25(2), 409-416 (2009-02-28)
Aspergillus niger lipase (ANL) is an important biocatalyst in the food processing industry. However, there is no report of its detailed three-dimensional structure because of difficulties in crystallization. In this article, based on experimental data and bioinformational analysis results, the
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
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