Purification, characterization and thermal inactivation kinetics of β-galactosidase from Lactobacillus leichmannii 313

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Title

Purification, characterization and thermal inactivation kinetics of β-galactosidase from Lactobacillus leichmannii 313

Content partner

University of Otago

Collection

Otago University Research Archive

Description

β-galactosidase from Lactobacillus leichmannii 313 (LL313) was purified (4.5-fold, 11% purification yield), and characterised, giving optimal enzyme activity at pH 5.5 and 55 °C. Thermal inactivation of crude and purified enzyme showed first order inactivation kinetics. Deactivation energy (Ed) of 390.58 ± 34.94 kJ/mol (crude enzyme) and 404.17 ± 46.19 kJ/mol (purified enzyme), based on the Arrhenius equation were not significantly different. Thermal stability, determined by decimal reduction...

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Format

Research paper

Research format

Scholarly text / Journal article

Thesis level

Article

Date created

2019-12

Creator

Ji, Dawei / Oey, Indrawati / Agyei, Dominic

URL

https://hdl.handle.net/10523/27666

Related subjects

Biochemical properties / Enzyme purification / Lactobacillus leichmannii 313 / Thermal properties / β-galactosidase

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