Enzyme-support interactions and inactivation conditions determine Thermomyces lanuginosus lipase inactivation pathways: Functional and florescence studies

Enzyme-support interactions and inactivation conditions determine Thermomyces lanuginosus lipase inactivation pathways: Functional and florescence studies

Lipase from Thermomyces lanuginosus (TLL) has been covalently immobilized on heterofunctional octyl-vinyl agarose. That way, the covalently immobilized enzymes will have identical orientation. Then, it has blocked using hexyl amine (HEX), ethylenediamine (EDA), Gly and Asp. The initial activity/stab...

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Bibliographic Details
Main Authors: Carballares, D. (Author), Fernandez-Lafuente, R. (Author), Gonçalves, L.R.B (Author), Lopez-Carrobles, N. (Author), Lopez-Gallego, F. (Author), Rodrigues, S. (Author), Souza, P.M.P (Author)
Format: Article
Language:English
Published: Elsevier B.V. 2021
Subjects:
Article
aspartic acid
Aspartic Acid
biocatalyst
chemistry
divinyl sulfone
enzyme activity
enzyme immobilization
enzyme inactivation
Enzyme inactivation under different conditions
enzyme specificity
enzyme stability
Enzyme tuning by immobilization
Enzymes, Immobilized
Enzyme-support interaction
enzymology
ethylenediamine
ethylenediamine derivative
Ethylenediamines
Eurotiales
fluorescence
fungal protein
Fungal Proteins
glycine
Glycine
immobilized enzyme
Inactivation of enzymes
Lipase
Lipase interfacial activation
metabolism
microsphere
Microspheres
nonhuman
pH
physical activity
scanning electron microscopy
sepharose
Sepharose
structure analysis
Substrate specificity
Substrate Specificity
sulfone
Sulfones
Thermomyces lanuginosus
thermostability
triacetin
Triacetin
triacylglycerol lipase
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