1998
DOI: 10.1111/j.1365-2621.1998.tb15755.x
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Functional Properties and Bitterness of Sodium Caseinate Hydrolysates Prepared with a Bacillus Proteinase

Abstract: The functional and physicochemical characteristics, and bitterness were evaluated on sodium caseinate hydrolysates generated with a commercial Bacillus proteinase complex. At low degrees of hydrolysis (0.5 and 1.0% DH) the hydrolysates compared to the unhydrolyzed substrate had increased emulsion activity at pH 2 and 4. However, higher DH resulted in lower emulsion activities. At pH 8 and 10, the low DH hydrolysates displayed increased foam expansion and decreased foam drainage compared to the starting substra… Show more

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Cited by 62 publications
(49 citation statements)
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“…The lowest solubility of all hydrolysates was achieved at pH 4.0 because the isoelectric point of Roselle seed protein is between 3.5 and 4, and the minimum solubility usually occurs at isoelectric point. Thus, the hydrolysis might be responsible for the increased solubility at the isoelectric point and at other pH levels as a result of shortening of molecular chains and the increase in the amount of polar groups (Chobert et al, 1988;Nielsen, 1997;Slattery and Fitzgerald, 1998). This trend in solubility is in agreement with previous reports (Clemente et al, 1999;Aluko and Monu, 2003).…”
Section: Nitrogen Solubility (Ns)supporting
confidence: 90%
See 1 more Smart Citation
“…The lowest solubility of all hydrolysates was achieved at pH 4.0 because the isoelectric point of Roselle seed protein is between 3.5 and 4, and the minimum solubility usually occurs at isoelectric point. Thus, the hydrolysis might be responsible for the increased solubility at the isoelectric point and at other pH levels as a result of shortening of molecular chains and the increase in the amount of polar groups (Chobert et al, 1988;Nielsen, 1997;Slattery and Fitzgerald, 1998). This trend in solubility is in agreement with previous reports (Clemente et al, 1999;Aluko and Monu, 2003).…”
Section: Nitrogen Solubility (Ns)supporting
confidence: 90%
“…Nevertheless, it is clear that the FC may depend on the protein structure, molecular size and hydrophobicity of the hydrolysate (Martin et al, 2002), which also depend highly on the hydrolysis procedure and the parent protein from which they are obtained. The effect of hydrolysis on foam stability is dependent on the degree of hydrolysis (Althouse et al, 1995;Mutilangi et al, 1996;Slattery and Fitzgerald, 1998). The short chain molecules form a wicker interaction network, which result in to a less stable foam.…”
Section: Foaming Capacity and Foaming Stabilitymentioning
confidence: 99%
“…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%
“…At 5, 10, 15 and 20 % DH, the casein hydrolysates were 50, 84.8, 86 and 91 % soluble at pH=5.0, respectively. These results accorded with those of Slattery and Fitzgerald (1998), Chobert et al (1988a) and Wani et al (2014). The results indicated that the enzymatic hydrolysis of whey and casein protein concentrates by Papain improved the solubility of their hydrolysates.…”
Section: Protein Solubilitysupporting
confidence: 82%