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Sigma-Aldrich

Lipase from Rhizopus oryzae

powder (fine), ~10 U/mg

Sinonimo/i:

Lipase from Rhizopus arrhizus, Triacylglycerol acylhydrolase, Triacylglycerol lipase

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54

Forma fisica

powder (fine)

Livello qualitativo

Attività specifica

~10 U/mg

PM

Mr ~43000

Temperatura di conservazione

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-;
QWZUIMCIEOCSJF-CHHCPSLASA-N

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Descrizione generale

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.

Applicazioni

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.

Azioni biochim/fisiol

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.

Definizione di unità

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

Altre note

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

Pittogrammi

Health hazard

Avvertenze

Danger

Indicazioni di pericolo

Consigli di prudenza

Classi di pericolo

Resp. Sens. 1

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


Certificati d'analisi (COA)

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I clienti hanno visto anche

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)
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)
Lipase enzymes on graphene oxide support for high-efficiency biocatalysis
HermanovaS, et al.
Applied Materials Today, 5 (2016)
Rhizopus oryzae Lipase, a Promising Industrial Enzyme: Biochemical Characteristics, Production and Biocatalytic Applications
Lopez-Fernandez J, et al.
Catalysts, 10, 1277-1277 (2020)

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