Description
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.
Analysis Note
enzyme activity:
the optimum temperature is 40°C, the optimum pH is 7.2 (highly active from pH 6.5-7.5)
Other Notes
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)
