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62305

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:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

form

powder (fine)

Quality Level

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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This Item
L8525L1754L4277
Sigma-Aldrich

62305

Lipase from Rhizopus oryzae

Lipase from Candida rugosa lyophilized powder, ≥40,000 units/mg protein

L8525

Lipase from Candida rugosa

Lipase from Candida rugosa Type VII, ≥700 unit/mg solid

L1754

Lipase from Candida rugosa

Sigma-Aldrich

L4277

Lipase from Aspergillus oryzae

form

powder (fine)

form

lyophilized powder

form

lyophilized

form

lyophilized

mol wt

Mr ~43000

mol wt

-

mol wt

-

mol wt

-

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

200

Quality Level

200

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

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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T. Kim et al.
Enzyme and Microbial Technology, 11, 528-528 (1989)
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
Rhizopus oryzae Lipase, a Promising Industrial Enzyme: Biochemical Characteristics, Production and Biocatalytic Applications
Lopez-Fernandez J, et al.
Catalysts, 10, 1277-1277 (2020)
Lipase enzymes on graphene oxide support for high-efficiency biocatalysis
HermanovaS, et al.
Applied Materials Today, 5 (2016)
Effective and highly selective lipase-mediated synthesis of 2-monoolein and 1, 2-diolein in a two-phase system
Serrano-Arnaldos JM, et al.
Journal of Molecular Catalysis. B, Enzymatic, 112, 9-14 (2014)

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