Controlled Hydrolysis of Cheese Whey Proteins Using Trypsin and α-Chymotrypsin
| Autor: | Raquel L. C. Giordano, Célia M.A. Galvão, Rubens Monti, A. S. Silva, Marcos Franqui Custodio |
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| Rok vydání: | 2001 |
| Předmět: |
Whey protein
medicine.medical_treatment Bioengineering Lactoglobulins Applied Microbiology and Biotechnology Biochemistry Substrate Specificity Enzyme catalysis Hydrolysis Cheese Enzyme Stability medicine Chymotrypsin Trypsin Molecular Biology Beta-lactoglobulin chemistry.chemical_classification Protease Chromatography biology food and beverages General Medicine Milk Proteins Whey Proteins Enzyme chemistry biology.protein Peptides Biotechnology medicine.drug |
| Zdroj: | Applied Biochemistry and Biotechnology. :761-776 |
| ISSN: | 0273-2289 |
| DOI: | 10.1385/abab:91-93:1-9:761 |
| Popis: | This study examined the production of protein hydrolysates with controlled composition from cheese whey proteins. Cheese whey was characterized and several hydrolysis experiments were made using whey proteins and purified beta-lactoglobulin, as substrates, and trypsin and alpha-chymotrypsin, as catalysts, at two temperatures and several enzyme concentrations. Maximum degrees of hydrolysis obtained experimentally were compared to the theoretical values and peptide compositions were calculated. For trypsin, 100% of yield was achieved; for alpha-chymotrypsin, hydrolysis seemed to be dependent on the oligopeptide size. The results showed that the two proteases could hydrolyze beta-lactoglobulin. Trypsin and alpha-chymotrypsin were stable at 40 degrees C, but a sharp decrease in the protease activity was observed at 55 degrees C. |
| Databáze: | OpenAIRE |
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