Interactions of milk proteins during heat and high hydrostatic pressure treatments — A Review

Considine, Thérèse; Patel, Hasmukh A.; Anema, Skelte G.; Singh, Harjinder; Creamer, Lawrence K.

doi:10.1016/j.ifset.2006.08.003

Cited by 295 publications

(220 citation statements)

References 157 publications

(228 reference statements)

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“…2E). With HPP and further re-heating, the globular pea proteins might 239 have been fully unfolded, allowing the otherwise buried hydrophobic groups to be exposed to 240 pepsin (Considine, et al, 2007). Therefore, in comparison with autoclaving, HPP followed by 241 re-heating showed highest kinetics and extent of gastric digestion ( Fig.…”

mentioning

confidence: 99%

In vitro gastrointestinal digestion of pea protein isolate as a function of pH, food matrices, autoclaving, high-pressure and re-heat treatments

Laguna

Picouet

Guárdia

et al. 2017

LWT

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confidence: 99%

In vitro gastrointestinal digestion of pea protein isolate as a function of pH, food matrices, autoclaving, high-pressure and re-heat treatments

Laguna

Picouet

Guárdia

et al. 2017

LWT

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“…The bubbles that formed because of cavitation fracture and instantly generate strong shear forces. The shearing changes the structure of proteins and exposes certain groups, which improves contact with enzymes and the antioxidant activity of the hydrolysate (Considine et al 2007). Compare with the thermal treatment, the ultrasonication increased the DPPH radical scavenging activity of highly denatured soybean meal hydrolysate by 8.31 % and its reduction capacity by 10.19 %.…”

Section: Resultsmentioning

confidence: 99%

“…Only small amounts of highly denatured soybean meal is used for production of fermented foods, resulting to a huge waste of high-quality proteins and physiologically active substances (Wang and Johnson 2001). Physical modification changes the structure of proteins, thereby improving the efficiency of enzymolysis and improving their functional properties (Considine et al 2007;Liu and Zhao 2010). Wu et al (2010) reported the antioxidant effect of soybean isolate protein enzymatic hydrolysate treated by ultrasonic.…”

Section: Introductionmentioning

confidence: 99%

Antioxidant activity and anti-exercise-fatigue effect of highly denatured soybean meal hydrolysate prepared using neutrase

2013

J Food Sci Technol

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Highly denatured soybean meal is a by-product of soybean oil extraction obtained through high-temperature desolventization. High-temperature treatment can result in soybean protein denaturation. Compare with ordinary soybean meal, the protein structure of highly denatured soybean meal has changed. Highly denatured soybean meal was pretreated with thermal treatment or ultrasonication, and then hydrolyzed with neutrase. The ultrasonicated hydrolysate exhibited better antioxidant activity than the thermally treated hydrolysate. The ultrasonication increased 1,1-diphenyl-2-pycryl hydrazyl (DPPH) radical scavenging activity by 8.31 % and reduction capacity by 10.19 %. The highly denatured soybean meal hydrolysate ultrasonicated at 400 W exhibited the highest antioxidant activity. The DPPH radical scavenging activity was 56.22 % and reduction capacity was 0.717. The ultrasonicated hydrolysate at 400 W was fractionated using ultrafiltration into three fractions: I (>10 kDa), II (5 kDa to 10 kDa), and III (<5 kDa). The in vitro antioxidant activity and others in vivo anti-exercise-fatigue effect of the three fractions (I, II, and III) were determined. Fraction III exhibited the highest DPPH radical scavenging activity and reduction capacity, improved the hemoglobin and hepatic glycogen content and reduced blood urea nitrogen and blood lactic acid. Fraction III improved the activity of superoxide dismutase (SOD) and glutathione peroxidase (GSH-PX) and reduced the malonaldehyde (MDA) content in mouse livers. Therefore, the highly denatured soybean meal hydrolysate has an anti-oxidative effect and it significantly alleviates exercisefatigue in mice. Amino acids of hydrolysate were determined.Results showed that the antioxidant activity and anti-exercisefatigue effect were related to the amino acid compositions.

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“…The influence of heating on proteolysis is determined by the level of temperature and duration of heating. It is well known that heating of milk above 70 °C induces denaturation of proteins, their re-assotiation into the so-called whey protein-casein complexes (WP-CN) mainly throught disulphide and hydrophobic interactions (Maćej et al, 2007;Considine et al, 2007). WP-CN complexes could be formed between serum proteins and caseins, mostly between β-lg, α-la and κ-CN (Considine et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

“…It is well known that heating of milk above 70 °C induces denaturation of proteins, their re-assotiation into the so-called whey protein-casein complexes (WP-CN) mainly throught disulphide and hydrophobic interactions (Maćej et al, 2007;Considine et al, 2007). WP-CN complexes could be formed between serum proteins and caseins, mostly between β-lg, α-la and κ-CN (Considine et al, 2007). These complexes could form molecules of major whey proteins alone, but also other whey proteins and caseins (a part of α s -and β-CN) could be incorporated in them (Chevalier et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Protein profiles and total antioxidant capacity of water soluble and insoluble protein fractions of white cow cheese at different stage of ripening

Barać

2016

Mljekarstvo

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This research is focused on proteolysis and total antioxidant capacity of proteins of white brined cheese prepared from overheated (90 °C, 10 minutes) cow milk. White brined cow cheese of overheated milk went through specific proteolytic changes during ripening that were result of high level of whey proteins incorporated into the gel matrix. Specificity was reflected through the relatively low level of soluble nitrogen fractions, the intensive and continual decrease of α s -caseins up to 15.42 % of initial content, slow degradation of β-casein throughout the whole ripening period and high level of proteolytic products tightly bounded into gel matrix. Strong negative correlations (-0.97, -0.98 and -0.91; p<0.05) between ripening time and resudual α s -caseins, β-casein and low molecular weight products were observed. Proteolysis also affected the total antioxidant capacity of both water soluble and water insoluble nitrogen fractions, but to different extents and with different trends. Total antioxidant capacity of water insoluble fraction increased slowly during the whole ripening period, wherease significant improvement of total antioxidant capacity of water soluble fraction started after 30 days of ripening. These findings could be useful for better understanding and control of the white brined cow cheese production.

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Interactions of milk proteins during heat and high hydrostatic pressure treatments — A Review

Cited by 295 publications

References 157 publications

In vitro gastrointestinal digestion of pea protein isolate as a function of pH, food matrices, autoclaving, high-pressure and re-heat treatments

In vitro gastrointestinal digestion of pea protein isolate as a function of pH, food matrices, autoclaving, high-pressure and re-heat treatments

Antioxidant activity and anti-exercise-fatigue effect of highly denatured soybean meal hydrolysate prepared using neutrase

Protein profiles and total antioxidant capacity of water soluble and insoluble protein fractions of white cow cheese at different stage of ripening

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