ArticleApplied biochemistry and biotechnology2021
Production and immobilization of β-galactosidase isolated from Enterobacter aerogenes KCTC2190 by entrapment method using agar-agar organic matrix.
Article in Applied biochemistry and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 17 citations in OpenAlex.
- Galactooligosaccharides Based on β-Galactosidase-Catalyzed Synthesis: Function, Biosynthesis and Optimization Strategy.Foods (Basel, Switzerland) · 2026Review
- Pros and Cons in Various Immobilization Techniques and Carriers for Enzymes.Applied biochemistry and biotechnology · 2024Review
- Glutaraldehyde-pea protein grafted polysaccharide matrices for functioning as covalent immobilizers.Scientific reports · 2023Article
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3 authors at 1 institution in 1 country.
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Abstract
In the present study, Enterobacter aerogenes KCTC2190 was isolated from soil around a cattle shed area, which was capable of producing intracellular β-galactosidase. Partially purified β-galactosidase was immobilized by entrapment method in agar-agar gel matrix. Agar-agar entrapped beads were prepared by dropping the enzyme-agar solution to ice-cooled toluene-chloroform ((3:1 (v/v)). 45.88±0.11% activity of partially purified β-galactosidase was retained after immobilization (bead shape). Maximum immobilization yield was observed in the presence of 2.5% agar-agar concentration. After immobilization, optimum temperature required for the enzyme-substrate reaction was shifted from 50 to 60 °C and the optimum reaction time was shifted from 15 to 25 min. The optimum pH for both free and immobilized β-galactosidase was pH 7. Free enzyme showed lower activation energy in comparison with the immobilized one. For free as well as immobilized β-galactosidase thermal deactivation, rate constant (k
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