General description
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.
Application
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.
Biochem/physiol Actions
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.
Unit Definition
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
Other Notes
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
- UPC:
- 12352204
- Condition:
- New
- Weight:
- 1.00 Ounces
- HazmatClass:
- No
- WeightUOM:
- LB
- MPN:
- 62305-1G-F
