2015
DOI: 10.1016/j.foodhyd.2015.01.007
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Characterizing the structural and surface properties of proteins isolated before and after enzymatic demulsification of the aqueous extract emulsion of peanut seeds

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Cited by 60 publications
(38 citation statements)
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References 46 publications
(61 reference statements)
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“…Unlikely, the EAI of bromelain hydrolysate was markedly increased by protein hydrolysis (P < 0.05), mainly in the second half of reaction time, possibly attributing to the molecular exibility of polypeptides and the exposure of hydrophobic areas. 29 However, no obvious uctuation of ESI was observed in emulsion stabilized by bromelain hydrolysates along with the progress of hydrolysis, excluding 180 min hydrolysis time. The highest ESI value of 78.11 h was found in the 180 min-bromelain-treated hydrolysate, which might be due to its high hydrophobicity and secondary structure.…”
Section: Surface Charge (Z-potential) and Emulsifying Propertiesmentioning
confidence: 97%
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“…Unlikely, the EAI of bromelain hydrolysate was markedly increased by protein hydrolysis (P < 0.05), mainly in the second half of reaction time, possibly attributing to the molecular exibility of polypeptides and the exposure of hydrophobic areas. 29 However, no obvious uctuation of ESI was observed in emulsion stabilized by bromelain hydrolysates along with the progress of hydrolysis, excluding 180 min hydrolysis time. The highest ESI value of 78.11 h was found in the 180 min-bromelain-treated hydrolysate, which might be due to its high hydrophobicity and secondary structure.…”
Section: Surface Charge (Z-potential) and Emulsifying Propertiesmentioning
confidence: 97%
“…Thereaer, as the hydrolysis time increased, these exposed hydrophobic groups was re-buried by their aggregation via hydrophobic interactions or increased protein exibility, resulting in the declination of hydrophobicity in hydrolysates. 8,29,30 The difference between cin and bromelain hydrolysates might due to DH and enzyme specicity, which determined the cleavage of peptide bonds and the exposure of hydrophobic residues.…”
Section: Emission Uorescence Spectroscopic Analysismentioning
confidence: 99%
“…Co., Ltd., Watertown, CT, USA) and milled into powder using a multipurpose electric grinder (HK-230, Kaichuang Tonghe Co., Beijing, China), and sieved through a 150 mesh screen. The free sulfhydryl-groups (-SH-) were determined 23 as follows: 150 mg dough powder suspended in 1 mL Tris-gly buffer (pH 8.0), 4.7 g guanidine hydrochloride was added and brought to 10 mL with buffer. After stirring for 25 min, 1 mL was mixed with 5 mL 8 M urea solution and 0.04 mL 4 mg/mL Ellman's reagents and kept at 25 °C for 30 min.…”
Section: Determination Of the Disulfide Content In Dough Dough Samplmentioning
confidence: 99%
“…Peanut protein and rice bran protein have not only high nutritional value, but also their functional characteristics which have attracted people’s attention [23]. Zhang and Lu (2015) found that peanut protein adsorbed on the oil/water interface in emulsions possessed higher emulsification [24]. Zhang et al (2017) have demonstrated that ultrasound treatment could unfold the conformation of rice bran protein, exposing its interior functional groups, which were related to its emulsifying property [25].…”
Section: Introductionmentioning
confidence: 99%