ArticleWorld journal of microbiology & biotechnology2020
Enhancement of biochemical aspects of lipase adsorbed on halloysite nanotubes and entrapped in a polyvinyl alcohol/alginate hydrogel: strategies to reuse the most stable lipase.
Article in World journal of microbiology & biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 20 citations in OpenAlex.
- Multi enzyme production and alginate encapsulation from Bacillus subtilis for stable feed additives.Scientific reports · 2025Article
- A Novel Method for γ-Aminobutyric Acid Biosynthesis Using Glutamate Decarboxylase Entrapped in Polyvinyl Alcohol-Sodium Alginate Capsules.Molecules (Basel, Switzerland) · 2023Article
- Immobilization of Lipases Using Poly(vinyl) Alcohol.Polymers · 2023Review
- Recent Advances of Macromolecular Hydrogels for Enzyme Immobilization in the Food Products.Advanced pharmaceutical bulletin · 2022Review
- Article
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Entrapment of halloysite nanotubes (HNTs) loaded with enzyme, into a polymer matrix (PVA/Alg), is a way to produce an environment surrounding the adsorbed enzyme molecules which improves the enzyme properties such as storage and operational stability. Hence, in this study, we optimised the factors affecting lipase adsorption onto halloysite nanotubes including halloysite amounts (5, 42.5 and 80 mg), lipase concentrations (30, 90 and 150 µg/ml), temperatures (5, 20 and 35 °C) and adsorption times (30, 165 and 300 min). The optimal conditions were determined as an halloysite amount of 50 to 80 mg, a lipase concentration of 30 to 57 μg/ml, an adsorption temperature of 20 °C and an adsorption time of 165 min, which resulted in a specific activity and adsorption efficiency of 15,000 (U/g protein) and 70%, respectively. Then, lipase adsorbed under optimal conditions was entrapped in a PVA/Alg hydrogel. The formation mechanism of immobilized lipase was investigated by FESEM and FTIR. Subsequent entrapment of adsorbed lipase improved the lipase storage and operational stability. K
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