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Sigma-Aldrich

Lipase from Rhizopus oryzae

powder (fine), ~10 U/mg

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Synonym(s):
Lipase from Rhizopus arrhizus, Triacylglycerol acylhydrolase, Triacylglycerol lipase
CAS Number:
9001-62-1
Enzyme Commission number:
3.1.1.3 (BRENDA, IUBMB)
EC Number:
232-619-9
MDL number:
MFCD00131509
NACRES:
NA.54

form

powder (fine)

Quality Level

100

specific activity

~10 U/mg

mol wt

Mr ~43000

storage temp.

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

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General description

Lipase from Rhizopus oryzae (ROL) comprises an oxyanion hole, four N-glycosylation sites, and an active site region. It possesses N-terminal presequence and prosequence.

Application

Lipase from Rhizopus oryzae has been used:
  • to test its effect on 1,2-diolein synthesis and triolein ethanolysis
  • for immobilization on graphene oxide support for biocatalysis studies
  • to digest triglycerides (TAG) from Chlamydomonas reinhardtii and S. cerevisiae

Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

Biochem/physiol Actions

Lipase from Rhizopus oryzae (ROL) acts as a catalyst for the enzymatic biosynthesis of polyglycerol polyricinoleate through a reversal of hydrolysis. ROL is useful in the industrial production of structured lipids due to its 1,3-regiospecificity functionality.
Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).

Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 μmol of butyric acid per minute at pH 8.0 and 40°C (tributyrin, Cat. No. 91010 as substrate) 5000 U as described above are equivalent to ~1 U using triolein, Cat. No. 62314 as substrate, at pH 8.0 and 40°C

Other Notes

Note: When triacetin is used as substrate, the pH is 7.4. Incubation time: 60 minutes.
Catalyst for the interesterification of oils and fats; For removal of interfering triglycerides in the electroimmunoassay of apolipoprotein B; Racemic epoxy ester resolution through enantioselective enzymatic hydrolysis

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Electroimmunoassay of apolipoprotein B in triacylglycerol-rich serum.
P Laburre et al.
Clinical chemistry, 31(5), 787-787 (1985-05-01)
Yeongho Kim et al.
Proceedings of the National Academy of Sciences of the United States of America, 115(7), 1652-1657 (2018-02-01)
Understanding the unique features of triacylglycerol (TAG) metabolism in microalgae may be necessary to realize the full potential of these organisms for biofuel and biomaterial production. In the unicellular green alga Chlamydomonas reinhardtii a chloroplastic (prokaryotic) pathway has been proposed
Lipase enzymes on graphene oxide support for high-efficiency biocatalysis
HermanovaS, et al.
Applied Materials Today, 5 (2016)
Rhizopus oryzae Lipase, a Promising Industrial Enzyme: Biochemical Characteristics, Production and Biocatalytic Applications
Lopez-Fernandez J, et al.
Catalysts, 10, 1277-1277 (2020)
T. Kim et al.
Enzyme and Microbial Technology, 11, 528-528 (1989)
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