Improvement of Digestibility of Bovine Serum Albumin by Chemical Treatment and Reduction in the Antigenicity of the Digests
| Autor: | Yumi Gotoh, Masakazu Tsutsumi, Yoshikazu Adachi, Yuji Miyaguchi |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Marketing
chemistry.chemical_classification Antigenicity Chromatography Protease biology General Chemical Engineering Sodium medicine.medical_treatment chemistry.chemical_element Industrial and Manufacturing Engineering chemistry.chemical_compound chemistry Biochemistry Thiol Urea biology.protein medicine Bovine serum albumin Hydrogen peroxide Food Science Biotechnology Cysteine |
| Zdroj: | Food Science and Technology Research. 7:149-153 |
| ISSN: | 1881-3984 1344-6606 |
| DOI: | 10.3136/fstr.7.149 |
| Popis: | Bovine serum albumin (BSA) was chemically treated in the presence or absence of L-cysteine (Cys) after the cleavage of hydrogen bonds by urea and reduction of disulfide linkages by sodium tetrahydroborate. The reduced BSA was re-oxidized with hydrogen peroxide and Cys treated- or non-Cys treated- BSA was obtained (C-BSA or NC-BSA). The percentage of thiol groups modified in C-BSA was 73.6%. The peptic digestibility of BSA was markedly improved by chemical treatment in the presence of Cys. The pancreatic and tryptic digestibility of BSA was higher in the order of C-BSA>NC-BSA>native BSA. SDS-PAGE confirmed that chemical treatment with Cys improved the digestibility of BSA and facilitated protein fragmentation into small molecular weight peptides by protease. Further, enzyme-linked immunosorbent assay showed that the antigenicity of the tryptic digests of BSA was reduced about one-tenth by the chemical treatment with Cys. This result indicated that the change in conformation of BSA decreased the antigenicity through enhancement of protease susceptibility. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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