The modification of slightly soluble sunflower protein isolates by superlimited proteolysis (-0.1 % splitting of the peptide bonds) raises 1 S-2-fold their solubility in neutral medium. The modified preparations may be isolated by isoelectric precipitation with a yield of 95-98 % and became capable
Modification of rheological properties of whey protein isolates by limited proteolysis
โ Scribed by Huang, X. L. ;Catignani, G. L. ;Swaisgood, H. E.
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 392 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0027-769X
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โฆ Synopsis
Whey protein isolate (WPI) was subjected to limited tryptic hydrolysis and the effect of the limited hydrolysis on the rheological properties of WPI was examined and compared with those of untreated WPI. At 10% concentration (w/v in 50 mM TES buffer, pH 7.0, containing 50 mM NaCl), both WPI and the enzyme-treated WPI (EWPI) formed heat-induced viscoelastic gels. However, EWPI formed weaker gels (lower storage modulus) than WPI gels. Moreover, a lower gelation point (77 ยฐC) was obtained for EWPI as compared with that of WPI which gelled at 80 ยฐC only after holding 1.4 min. Thermal analysis and aggregation studies indicated that limited proteolysis resulted in
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