Study on immobilizing of lipase on the superabsorbent
Jin Ze
Abstract
Jin Ze
Abstract
Lipase was immobilized on the super absorbent polymer by physical absorption and covalence,and the immobilized lipase was compared with the free lipase.The results show that the optimum pH of the free lipase,was 7.0 and lower than that of the immobilized lipase(pH7.5 or pH8.0).The optimum reaction temperature shifted from 40 ℃ for the free lipase to 45 ℃ or 50 ℃ for the immobilized lipase.In comparison with free lipase,the thermal and acid-basic stability of immobilized lipase was increased.
A significance statement is not available in the OpenAlex record.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
Lipase was immobilized on the super absorbent polymer by physical absorption and covalence,and the immobilized lipase was compared with the free lipase.The results show that the optimum pH of the free lipase,was 7.0 and lower than that of the immobilized lipase(pH7.5 or pH8.0).The optimum reaction temperature shifted from 40 ℃ for the free lipase to 45 ℃ or 50 ℃ for the immobilized lipase.In comparison with free lipase,the thermal and acid-basic stability of immobilized lipase was increased.
Key concepts: Lipase, Chemistry, Immobilized enzyme, Absorption capacity, Chromatography, Triacylglycerol lipase, Covalent bond, Enzyme