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Merck

80612

Sigma-Aldrich

Lipase aus Rhizopus oryzae

powder, light brown, ≥30 U/mg

Synonym(e):

Lipase F-AP 15

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About This Item

CAS-Nummer:
EC-Nummer:
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

fungus (Rhizopus oryzae)

Form

powder

Spezifische Aktivität

≥30 U/mg

Farbe

light brown

Lagertemp.

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-;

InChIKey

QWZUIMCIEOCSJF-CHHCPSLASA-N

Allgemeine Beschreibung

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.

Anwendung

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. Wirkung

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.

Einheitendefinition

1 U entspricht der Enzymmenge, die 1 μmol Fettsäure aus Triglyceriden pro Minute bei pH 7.2 und 37°C freisetzt (Olivenöl als Substrat)

Hinweis zur Analyse

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

Piktogramme

Health hazard

Signalwort

Danger

H-Sätze

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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)
Lysine blockage of milk proteins in infant formula impairs overall protein digestibility and peptide release
Zenker HE, et al.
Food & Function, 358-369 (2020)
Highly efficient enzymatic biodiesel production promoted by particle-induced emulsification
Mangas-S'anchez J and Adlercreutz P
Biotechnology for Biofuels (2015)
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)
Production of Rhizopus oryzae lipase using optimized Yarrowia lipolytica expression system
Vidal L, et al.
FEMS Yeast Research, 23 (2023)

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