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Merck

62305

Sigma-Aldrich

Lipase from Rhizopus oryzae

powder (fine), ~10 U/mg

Sinónimos:

Lipase from Rhizopus arrhizus, Triacylglycerol acylhydrolase, Triacylglycerol lipase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

Formulario

powder (fine)

Nivel de calidad

actividad específica

~10 U/mg

mol peso

Mr ~43000

temp. de almacenamiento

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-;

Clave InChI

QWZUIMCIEOCSJF-CHHCPSLASA-N

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Descripción general

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.

Aplicación

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.

Acciones bioquímicas o fisiológicas

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.

Definición de unidad

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

Otras notas

Note: When triacetin is used as substrate, the pH is 7.4. Incubation time: 60 minutes.
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

Pictogramas

Health hazard

Palabra de señalización

Danger

Frases de peligro

Consejos de prudencia

Clasificaciones de peligro

Resp. Sens. 1

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


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Visite la Librería de documentos

T. Kim et al.
Enzyme and Microbial Technology, 11, 528-528 (1989)
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)
Yeongho Kim et al.
Proceedings of the National Academy of Sciences of the United States of America, 115(7), 1652-1657 (2018-02-01)
Understanding the unique features of triacylglycerol (TAG) metabolism in microalgae may be necessary to realize the full potential of these organisms for biofuel and biomaterial production. In the unicellular green alga Chlamydomonas reinhardtii a chloroplastic (prokaryotic) pathway has been proposed
Lipase enzymes on graphene oxide support for high-efficiency biocatalysis
HermanovaS, et al.
Applied Materials Today, 5 (2016)
Effective and highly selective lipase-mediated synthesis of 2-monoolein and 1, 2-diolein in a two-phase system
Serrano-Arnaldos JM, et al.
Journal of Molecular Catalysis. B, Enzymatic, 112, 9-14 (2014)

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