Influence of milk proteins on the thermostability of the lipase from Pseudomonas fluorescens 33.
The effects of some milk proteins on the thermostability of the lipase from Pseudomonas fluorescens 33 were investigated. All purified milk protein fractions except kappa-casein that dissolved in phosphate buffer were effective for thermostabilization of the lipase. Thermal behavior of the lipase containing beta-lactoglobulin was so specific that, after heating at 80 to 90 degrees C, activity remained high and was comparable with that of unheated treatment. The thermostability of the lipase containing whey proteins in synthetic salts solution was extensively lowered, but that containing casein micelles retained 50% of original activity after heat treatment at 80 degrees C for 10 min. Low temperature inactivation of the lipase was influenced by concomitant milk proteins.
Kumura
H
H
Laboratory of Dairy Science, Faculty of Agriculture, Hokkaido University, Sapporo, Japan.
Mikawa
K
K
Saito
Z
Z
D002364:Caseins / Q000494:pharmacology; D004795:Enzyme Stability; D006358:Hot Temperature; D007782:Lactoglobulins / Q000494:pharmacology; D008049:Lipase / Q000378:metabolism*; D008894:Milk Proteins / Q000494:pharmacology*; D011551:Pseudomonas fluorescens / Q000201:enzymology*; D000067816:Whey Proteins
D002364:Caseins; D007782:Lactoglobulins; D008894:Milk Proteins; D000067816:Whey Proteins; D008049:Lipase