Lipase from Rhizopus oryzae

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.

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.

Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

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

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.

Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).

Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.

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.

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

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.

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