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80612

Sigma-Aldrich

Lipase from Rhizopus oryzae

powder, light brown, ≥30 U/mg

Synonym(s):

Lipase F-AP 15

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

fungus (Rhizopus oryzae)

form

powder

specific activity

≥30 U/mg

color

light brown

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

General description

Research Area: CELL SIGNALING,Rhizopus oryzae lipase (ROL) is a protein synthesized in a precursor form that includes a 26-amino acid presequence, followed by a 97-amino acid prosequence attached to the N-terminal of a mature sequence consisting of 269 amino acids. ROL possesses four potential N-glycosylation sites and is characterized by nine α-helices and eight β-strands, resulting in a molecule stabilized by three disulfide bonds between residues 29–269, 40–43, and 235–244. Lipases are widely distributed in various living organisms, including animals, plants, and microbes.

Application

Lipase from Rhizopus oryzae has been used:
  • to replace rabbit gastric extract for infant in vitro digestion
  • in the two-phase lipase-catalyzed system for the enzymatic preparation of biodiesel
  • in the simulation of infant gastrointestinal digestion in vitro, focusing on the characteristics of emulsions during digestion to replicate the stomach environment and adjust the emulsion pH

Biochem/physiol Actions

Lipases play a crucial role in catalyzing the breakdown of ester bonds of triglycerides at the interface between aqueous and oily layers. The lipase produced by Rhizopus species is known for its suitability in various industrial applications. In industrial settings, lipases of microbial origin are commonly extracellular and are produced during the fermentation process. The utilization of lipases has been shown to be more effective than traditional chemical syntheses in industries such as pharmaceuticals, cosmetics, oleochemicals, detergents, and fragrances.
These enzymes are widely used to modify the structure of oils and fats, tailoring natural lipids to meet specific properties useful for food, nutrition, and cosmetic applications. Lipases from filamentous fungi families, such as Rhizopus oryzae are extensively utilized in the oil and fats industry due to their high 1,3-regioselectivity toward triglycerides, making them versatile in lipid modification. Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

Unit Definition

1 U corresponds to the amount of enzyme which releases 1 μmol fatty acid from triglycerides per minute at pH 7.2 and 37 C (olive oil as substrate)

Analysis Note

enzyme activity:
the optimum temperature is 40°C, the optimum pH is 7.2 (highly active from pH 6.5-7.5)

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Highly efficient enzymatic biodiesel production promoted by particle-induced emulsification
Mangas-S'anchez J and Adlercreutz P
Biotechnology for Biofuels (2015)
Changes in interfacial composition and structure of milk fat globules are crucial regulating lipid digestion in simulated in-vitro infant gastrointestinal digestion
Sun Y, et al.
Food Hydrocolloids, 134, 108003-108003 (2023)
Lipase from Rhizopus oryzae R1: in-depth characterization, immobilization, and evaluation in biodiesel production
Helal SE, et al.
Journal of Genetic Engineering and Biotechnology, 19(1), 1-1 (2021)
Lysine blockage of milk proteins in infant formula impairs overall protein digestibility and peptide release
Zenker HE, et al.
Food & Function, 358-369 (2020)
Michael Thomas Zumstein et al.
Environmental science & technology, 51(8), 4358-4367 (2017-02-01)
Biodegradable polyesters have the potential to replace nondegradable, persistent polymers in numerous applications and thereby alleviate plastic accumulation in the environment. Herein, we present an analytical approach to study enzymatic hydrolysis of polyesters, the key step in their overall biodegradation

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