62305
Lipase from Rhizopus oryzae
powder (fine), ~10 U/mg
Synonym(s):
Lipase from Rhizopus arrhizus, Triacylglycerol acylhydrolase, Triacylglycerol lipase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-619-9
MDL number:
Specific activity:
~10 U/mg
Product Name
Lipase from Rhizopus oryzae, powder (fine), ~10 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 (fine)
specific activity
~10 U/mg
mol wt
Mr ~43000
storage temp.
2-8°C
Quality Level
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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
Rhizopus oryzae lipase (ROL) has been extensively researched for its regiospecificity in biodiesel production. Due to its remarkable characteristics, including 1,3-specificity, high enantioselectivity, and stability in organic solvents, ROL has garnered significant attention for applications in the energy, food, and pharmaceutical industries.
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.
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
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.
Research Area: Cell Signaling
Rhizopus oryzae lipase (ROL) is a protein synthesized in a precursor form that includes a presequence of 26 amino acids, followed by a prosequence of 97 amino acids, which is attached to the N-terminal of a mature sequence consisting of 269 amino acids.
Rhizopus oryzae lipase (ROL) is a protein synthesized in a precursor form that includes a presequence of 26 amino acids, followed by a prosequence of 97 amino acids, which is attached to the N-terminal of a mature sequence consisting of 269 amino acids.
Other Notes
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
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.
Note: When triacetin is used as substrate, the pH is 7.4. Incubation time: 60 minutes.
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)
Regulatory Information
常规特殊物品
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Rhizopus oryzae lipase, a promising industrial enzyme: Biochemical characteristics, production and biocatalytic applications
L'opez-Fern'andez J, et al.
Catalysts (Basel, Switzerland), 1277-1277 (2020)
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)
Electroimmunoassay of apolipoprotein B in triacylglycerol-rich serum.
P Laburre et al.
Clinical chemistry, 31(5), 787-787 (1985-05-01)
T. Kim et al.
Enzyme and Microbial Technology, 11, 528-528 (1989)
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