2012
DOI: 10.1111/j.1365-2621.2012.02993.x
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Functional properties of protein hydrolysates from pea (Pisum sativum, L) seeds

Abstract: Summary The aim of this study was to investigate the effects of partial enzymatic hydrolysis on functional properties of two different pea protein isolates obtained from two pea genotypes, Maja and L1. Papain and commercial protease (Streptomyces griseus protease) were used for protein modification. Solubility, emulsifying and foaming properties were estimated at four different pH values (3.0, 5.0, 7.0 and 8.0). Papain increased solubility of L1 pea protein isolate at pH 3.0, 5.0 and 8.0, emulsifying propertie… Show more

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Cited by 60 publications
(50 citation statements)
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References 36 publications
(67 reference statements)
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“…Some studies showed that an increase in the DH of the protein increased the solubility (Liu et al ., ; Intarasirisawat et al ., ); this may be due to the fact that the enzymatic hydrolysis can decrease the molecular size of protein by creating small peptides and unfolding the protein molecule, leading to more polar and ionisable groups being exposed on the protein surface, which could improve the protein molecule's ability to form hydrogen bonds with water and thereby augment solubility. However, other studies reported higher solubility of protein with lower DH (Tsoukala et al ., ; Barac et al ., ). This probably occurs because the protein molecule exposes more hydrophobic groups as the DH increases (Li et al ., ).…”
Section: Resultsmentioning
confidence: 97%
“…Some studies showed that an increase in the DH of the protein increased the solubility (Liu et al ., ; Intarasirisawat et al ., ); this may be due to the fact that the enzymatic hydrolysis can decrease the molecular size of protein by creating small peptides and unfolding the protein molecule, leading to more polar and ionisable groups being exposed on the protein surface, which could improve the protein molecule's ability to form hydrogen bonds with water and thereby augment solubility. However, other studies reported higher solubility of protein with lower DH (Tsoukala et al ., ; Barac et al ., ). This probably occurs because the protein molecule exposes more hydrophobic groups as the DH increases (Li et al ., ).…”
Section: Resultsmentioning
confidence: 97%
“…Foaming properties were expressed as foaming capacity (FC) and foam stability (FS) as described by Barac et al (2011Barac et al ( , 2012. Foaming was attained by bubbling a stream of air (6 dm 3 min −1 ) for 15 s through a Waters filter holder (Waters, USA) placed at the bottom of a 250 ml graduated column containing 30 ml 0.1 % protein solution in water adjusted to pH 3.0, 5.0, 7.0 and 8.0.…”
Section: Foaming Propertiesmentioning
confidence: 99%
“…In the case of native pea protein isolates, these differences were more pronounced and significant at all pH values. Barac et al (2010Barac et al ( , 2012 attributed these variations of solubility to protein composition of pea isolate and different nature of complexes formed during processing of isolate (during isoelectric precipitation) or during solubilization of isolate at specific pH.…”
Section: Protein Solubilitymentioning
confidence: 99%
“…This was demonstrated by work of Barac et al [78] who used papain and a commercial enzyme to hydrolyse pea protein isolate. While significant improvements in emulsifying properties, at least over some range of pH, was noticed for papain, the same was not true when the commercial enzyme was used.…”
Section: Fragmented Proteinsmentioning
confidence: 95%