Peptic hydrolysis of ovine β-lactoglobulin and α-lactalbumin Exceptional susceptibility of native ovine β-lactoglobulin to pepsinolysis

El-Zahar, Khaled; Sitohy, Mahmoud; Choiset, Yvan; Métro, François; Haertlé, Thomas; Chobert, Jean‐Marc

doi:10.1016/j.idairyj.2004.06.002

Cited by 46 publications

(30 citation statements)

References 35 publications

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“…After treatment with both HGJ and HDJ, image analysis of the gel showed that only small amounts (approximately 23%) of the caprine b-LG still remained undigested, while the amount of intact bovine b-LG was about 83%. Similar results from hydrolysis of ovine and bovine b-LG by commercial pepsin were obtained by El-Zahar et al (2005). Ovine b-LG was degraded faster due to its tertiary structure, and also surface hydrophobicity, being slightly different from those of bovine b-LG (El-Zahar et al, 2005).…”

Section: Discussionsupporting

confidence: 67%

“…Focus on genetic polymorphism of b-lactoglobulin (b-LG) and a-lactalbumin (a-LA) has revealed important differences between the bovine and caprine milk (Hill et al, 1997;Moatsou, Hatzinaki, Samolada, & Anifantakis, 2005;Trujillo, Casals, & Guamis, 2000). A recent study demonstrated major differences between hydrolysis of bovine and ovine b-LG by pepsin, due to small variations in the tertiary structure (El-Zahar et al, 2005). The ovine b-LG was hydrolysed faster.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

In vitro digestion of bovine and caprine milk by human gastric and duodenal enzymes

Almaas

Cases

Devold

et al. 2006

International Dairy Journal

131

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Section: Discussionsupporting

confidence: 67%

Section: Introductionmentioning

confidence: 99%

In vitro digestion of bovine and caprine milk by human gastric and duodenal enzymes

Almaas

Cases

Devold

et al. 2006

International Dairy Journal

131

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“…BLG variant B was more rapidly hydrolyzed by trypsin than BLG variant A, yielding about 70 and 44% hydrolysis, respectively, after 1 h of incubation. Nearly complete hydrolysis (95%) was obtained for the two variants after 24 h. Higher susceptibility of variant B to proteolysis was previously observed with pepsin [14]. The difference in susceptibility to trypsin hydrolysis reported here for the ovine BLG variants was also observed previously in the case of the variants of bovine BLG [23,37,50] and was attributed to structural differences between them.…”

Section: Tryptic Hydrolysis Of Blgsupporting

confidence: 85%

Angiotensin I-converting-enzyme (ACE)-inhibitory activity of tryptic peptides of ovine β-lactoglobulin and of milk yoghurts obtained by using different starters

Chobert¹,

El-Zahar²,

Sitohy³

et al. 2005

Lait

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-The aim of this study was to investigate the angiotensin I-converting-enzyme (ACE)-inhibitory activity of tryptic hydrolysates of ovine β-lactoglobulin, and of yoghurts made by using different starters. Ovine β-lactoglobulin (a mixture of variants A and B at a ratio of 50/50) was subjected to trypsin activity. The degree of hydrolysis of native whole β-lactoglobulin reached 56, 72, 93 and 95% after 1, 2, 8 and 24 h, respectively. ACE-inhibitory activity of tryptic hydrolysates increased with the time of hydrolysis, yielding 85, 88 and 92% after 2, 12 and 24 h, respectively. The determination of ACE-inhibitory activity of some tryptic peptides separated by RP-HPLC and identified by mass spectroscopy showed that the more hydrophilic peptides showed the higher activity. Yoghurts obtained by fermentation of ovine milk with four different sets of starters, and their fractions soluble or not at pH 4.6 also showed an ACE-inhibitory activity. The maximum activity was obtained in the case of insoluble fractions at pH 4.6 of yoghurts made with the set of starters YC-183. ovine milk / tryptic peptide / yoghurt / ACE-inhibitory activity Résumé -Activité inhibitrice de l'enzyme de conversion de l'angiotensine I (ECA) de peptides trypsiques de la β-lactoglobuline du lait de brebis et de yoghourts obtenus à partir de diffé-rents levains. Une activité inhibitrice de l'enzyme de conversion de l'angiotensine I (ECA) a été recherchée dans les peptides trypsiques de la β-lactoglobuline du lait de brebis et dans des fractions issues de yoghourts fabriqués à partir de différents ferments lactiques. La β-lactoglobuline ovine (un mélange des variants A et B) a été soumise à une hydrolyse trypsique. Les degrés d'hydrolyse de la β-lactoglobuline ont atteint 56, 72, 93 et 95 % respectivement après 1, 2, 8 et 24 h d'hydrolyse. L'activité inhibitrice de l'ECA des hydrolysats trypsiques augmentait avec la durée de l'hydrolyse, atteignant 85, 88 et 92 % respectivement après 2, 12 et 24 h. La détermination de l'activité inhibitrice de l'ECA de quelques peptides trypsiques séparés par CLHP en phase inversée et identifiés par spectrométrie de masse a montré que les peptides les plus hydrophiles présentaient l'activité la plus

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“…Moreover, though the β-Lg is generally resistant to human gastrointestinal enzymes, probably because of the binding of fatty acids in the barrel of the structure, resistance to peptic digestion is different among species, so that ovine β-Lg is far more digestible than bovine counterpart (El-Zahar et al 2005). Interestingly, donkey β-Lg is highly degraded (70%) in vitro by human gastric (HGJ) and duodenal juice (HDJ) (Tidona (2009) et al 2014) that is twice as much in comparison to cow counterpart (Inglistad et al 2010).…”

Section: β-Lactoglobulinmentioning

confidence: 99%

Whey proteins and their antimicrobial properties in donkey milk: a brief review

Brumini

Criscione

Bordonaro

et al. 2015

Dairy Sci. & Technol.

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Milk is a source of bioactive compounds essential for health and growth of newborns. Donkey milk, rich in lactose and whey proteins, has been proven to be a good breast milk substitute during infancy and adequate nourishment for patients with cow milk protein allergy. Beside, this milk is gaining a growing interest for human nutrition because of some other alleged health benefit. It shows antibacterial activity toward a wide range of Gram-positive and Gram-negative bacteria, stimulates immune system in convalescence, regulates gastrointestinal flora, and prevents inflammatory and autoimmune diseases. As regards its antimicrobial properties, although all the milk components might contribute to this activity, the whey protein fraction of donkey milk is generally believed to play the main role. The aim of this review is to highlight the antimicrobial properties of donkey milk with a special focus on the whey protein fraction. The effects of preservation and processing treatments on whey protein content and antimicrobial activity are also discussed.

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Peptic hydrolysis of ovine β-lactoglobulin and α-lactalbumin Exceptional susceptibility of native ovine β-lactoglobulin to pepsinolysis

Cited by 46 publications

References 35 publications

In vitro digestion of bovine and caprine milk by human gastric and duodenal enzymes

In vitro digestion of bovine and caprine milk by human gastric and duodenal enzymes

Angiotensin I-converting-enzyme (ACE)-inhibitory activity of tryptic peptides of ovine β-lactoglobulin and of milk yoghurts obtained by using different starters

Whey proteins and their antimicrobial properties in donkey milk: a brief review

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