Immobilization of glucose oxidase and horseradish peroxidase in biomimetic silica particles

ZHOU Ran; SONG Yu-pin; LIU Xiao-mei; XUN He-feng; HOU Dong-mei; WU Xin-rui; LIU Ling-jun

doi:10.13386/j.issn1002-0306.2017.02.034

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Science and Technology of Food Industry > 2017 > (02): 221-225. > DOI: 10.13386/j.issn1002-0306.2017.02.034

ZHOU Ran, SONG Yu-pin, LIU Xiao-mei, XUN He-feng, HOU Dong-mei, WU Xin-rui, LIU Ling-jun. Immobilization of glucose oxidase and horseradish peroxidase in biomimetic silica particles[J]. Science and Technology of Food Industry, 2017, (02): 221-225. DOI: 10.13386/j.issn1002-0306.2017.02.034

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Immobilization of glucose oxidase and horseradish peroxidase in biomimetic silica particles

School of Chemical Engineering,Shijiazhuang University
School of Chemical Engineering,Heibei University of Technology
Hebei San Yuan Food Co.,Ltd.

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Received Date: July 17, 2016

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Abstract

The fractional step method was applied to immobilize GOx and HRP by the combination of biomimetic silicification and liposome technology,using amine as an inducer,liposome as template.The time of ultrasonic,the dosage of PDADMA,the dosage of TMOS and the concentration of Triton X-100 on the effect of enzyme activity were studied.The results showed that the immobilized enzyme prepared with 200 μL PDADMA,0.7 m L TMOS,1% Triton X- 100 and 50 min for ultrasound had the highest activity.The results of SEM showed that immobilized enzyme particles were near- spheres,which were about 200 nm.The immobilized enzyme prepared under the optimal conditions could be of higher stability and recovery rate. The immobilized enzyme repeated seven cycles could still retain 61.46% of its initial activity.In the storage of the 30 days,the relative activity of immobilized GOx could still retain 74.1% of its initial activity. Thus,the stability of the double enzyme system has been significantly improved after immobilization.
- biomimetic silicification,
- liposome,
- glucose oxidase,
- horseradish peroxidase,
- nanosilica microcapsule

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