Enzymatic characterisation of the immobilised Alcalase to hydrolyse egg white protein for potential allergenicity reduction
| Autor: | Caiyun Long, Cheng Youfei, Jiaheng Xia, Yan Wang, Hongbing Chen, Ping Tong, Anshu Yang |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0106 biological sciences
chemistry.chemical_classification Nutrition and Dietetics Chromatography Immobilized enzyme Globulin biology Egg protein 02 engineering and technology 021001 nanoscience & nanotechnology 01 natural sciences Hydrolysate chemistry.chemical_compound Hydrolysis Enzyme chemistry 010608 biotechnology biology.protein 0210 nano-technology Agronomy and Crop Science Food Science Biotechnology Carbodiimide Egg white |
| Zdroj: | Journal of the Science of Food and Agriculture. 97:199-206 |
| ISSN: | 0022-5142 |
| DOI: | 10.1002/jsfa.7712 |
| Popis: | This study examined technique characteristics of the immobilised Alcalase to hydrolyse egg white protein for potential allergenicity reduction. Alcalase was immobilised covalently on carboxyl-functionalised magnetic beads by carbodiimide activation. The technique characteristics of the immobilised Alcalase were investigated, followed by determining the degrees of hydrolysis (DH), immunoglobulin G (IgG) binding, and IgE binding of the digested egg white protein by immobilised Alcalase. RESULTS Enzymatic activity, enzyme loading, and immobilisation yield of the prepared immobilised Alcalase were 20.55 U mg?1, 925?mg?g?1, and 45%, respectively. Immobilised Alcalase showed maximum activity at pH 8.0 and 60?°C. Compared with free Alcalase, immobilised Alcalase exhibited better thermal and storage stability. Moreover, immobilised Alcalase can be reused 10 times and still maintained 55% of its initial activity. Partial hydrolysis of egg white protein by immobilised Alcalase can effectively reduce IgG and IgE binding of the hydrolysates. CONCLUSION This study indicates that the immobilised Alcalase can be used to hydrolyse continuously egg white protein for potential allergenicity reduction. ? 2016 Society of Chemical Industry |
| Databáze: | OpenAIRE |
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