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80612

Sigma-Aldrich

Lipase from Rhizopus oryzae

powder, light brown, ≥30 U/mg

Synonyme(s) :

Lipase F-AP 15

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

fungus (Rhizopus oryzae)

Forme

powder

Activité spécifique

≥30 U/mg

Couleur

light brown

Température de stockage

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-;

Clé InChI

QWZUIMCIEOCSJF-CHHCPSLASA-N

Description générale

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

Actions biochimiques/physiologiques

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.

Définition de l'unité

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)

Remarque sur l'analyse

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

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

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)
Lysine blockage of milk proteins in infant formula impairs overall protein digestibility and peptide release
Zenker HE, et al.
Food & Function, 358-369 (2020)
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)
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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