1988
DOI: 10.1021/jf00083a002
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Solubility and emulsifying properties of caseins and whey proteins modified enzymically by trypsin

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Cited by 284 publications
(208 citation statements)
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“…They were from 84.8%~98% soluble between pH 4.0~5.0 at 10%~20% DH. These results accord with those of Slattery and Fitzgerald (1998), Chobert et al(1988a;1988b).…”
Section: Protein Solubilitysupporting
confidence: 91%
See 1 more Smart Citation
“…They were from 84.8%~98% soluble between pH 4.0~5.0 at 10%~20% DH. These results accord with those of Slattery and Fitzgerald (1998), Chobert et al(1988a;1988b).…”
Section: Protein Solubilitysupporting
confidence: 91%
“…It altered their structure and exposed previously buried hydrophobic regions to the aqueous environment. The enhanced solubility of sodium caseinate and WPC hydrolysates was also due to their smaller molecular size (data not shown) as confirmed by Chobert et al(1988b) and Mutilangi et al(1996). Although Protamex is an endopeptidase with a broad specificity to hydrophobic amino acids, it attacked WPC 80 and sodium caseinate at specific sites.…”
Section: Protein Solubilitymentioning
confidence: 74%
“…It altered their structure and exposed previously buried hydrophobic regions to the aqueous environment. The enhanced solubility of casein and WPC hydrolysates was also due to their smaller molecular size as confirmed by Chobert et al (1988b) and Mutilangi et al (1996).…”
Section: Protein Solubilitymentioning
confidence: 79%
“…protein solubility, emulsifying or foaming properties) by limited proteolysis of proteins in comparison to the native, nonhydrolysed protein as already shown for a variety of conventional proteins such as soy proteins [29], rape seed proteins [30] and milk proteins [31]. Similar studies investigating targeted enzymatic hydrolysis of insect proteins to enhance functional properties are scarce.…”
Section: Introductionmentioning
confidence: 99%