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LIPASE FROM RHIZOPUS NIVEUS ~1.5 U/MG (C15-1290-046)

Sigma Aldrich

Catalog No.
C15-1290-046
Manufacturer No.
62310-50G-F
Manufacturer Name
Sigma-Aldrich
Quantity
50
Unit of Measure
GR
Price: $461.33
List Price: $512.59

Lipases hydrolyze ester bonds of triacylglycerols and in some conditions, catalyze the synthesis of ester bonds by transesterification. Lipase from Rhizopus niveus exists as a single polypeptide chain with a molecular mass of about 30-34kDa.

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General description

Lipases hydrolyze ester bonds of triacylglycerols and in some conditions, catalyze the synthesis of ester bonds by transesterification. Lipase from Rhizopus niveus exists as a single polypeptide chain with a molecular mass of about 30-34kDa.

Application

Lipase from Rhizopus niveus has been used to determine the positional distribution of fatty acids within triacylglycerol by hydrolysis of the acyl ester linkage at C-1 and C-3. It has also been used to induce intragastric lipolysis and study its effects on felodipine (a medication) release from a hydrophilic, extended release tablet.

Biochem/physiol Actions

Lipase from Rhizopus niveus is specifically used to produce cocoa butter substitutes.

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

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 μmol fatty acid from a triglyceride per minute at pH 7.7 and 40°C (olive oil as substrate)]; 300 U as described above are equivalent to ~1 U using triolein, Cat. No. 62314, at pH 8.0 and 40°C as substrate.

Other Notes

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

Substrate specificity: preferentially hydrolyzes the 1- and 3-positions(middle to long fatty acids); optimum pH 5.0-7.0; optimum temperature 30-45°C; Selective enzymatic removal of protecting functions (C-terminal COOH function)

UPC:
12352200
Condition:
New
Weight:
1.00 Ounces
HazmatClass:
No
WeightUOM:
LB
MPN:
62310-50G-F

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