Thermal inactivation of immobilized lipase in 1-alcohols.
The thermal inactivation of immobilized lipase from Candida antarctica in 1-alcohols with four to eight carbons at various temperatures could be well expressed using a model in which heterogeneity in the susceptibility of the enzyme to the inactivation was assumed. It was found that the enthalpy-entropy compensation held for inactivation in 1-alcohols.
Yoshida
Yayoi
Y
Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
Kimura
Yukitaka
Y
Adachi
Shuji
S
D000438:Alcohols / Q000737:chemistry*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D005656:Fungal Proteins; D006358:Hot Temperature; D008049:Lipase / Q000032:analysis* / Q000737:chemistry*; D011489:Protein Denaturation; D012997:Solvents / Q000737:chemistry
D000438:Alcohols; D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D012997:Solvents; D008049:Lipase; C431349:lipase B, Candida antarctica