title: Thermal inactivation of immobilized lipase in 1-alcohols.
abstract: 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.
authors.affiliation: Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan.
authors.forename: Yayoi
authors.initials: Y
authors.lastname: Yoshida
authors.forename: Yukitaka
authors.initials: Y
authors.lastname: Kimura
authors.forename: Shuji
authors.initials: S
authors.lastname: Adachi
mesh_terms: 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
chemical_list: D000438:Alcohols; D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D012997:Solvents; D008049:Lipase; C431349:lipase B, Candida antarctica