62305
Lipase from Rhizopus oryzae
powder (fine), ~10 U/mg
Sinônimo(s):
Lipase from Rhizopus arrhizus, Triacylglycerol acylhydrolase, Triacylglycerol lipase
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About This Item
Produtos recomendados
forma
powder (fine)
Nível de qualidade
atividade específica
~10 U/mg
peso molecular
Mr ~43000
temperatura de armazenamento
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-;
chave InChI
QWZUIMCIEOCSJF-CHHCPSLASA-N
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Descrição geral
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.
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.
Aplicação
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.
Ações bioquímicas/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.
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
Definição da unidade
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
Outras 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
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Resp. Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
Certificados de análise (COA)
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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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