Hydrolysis of α-lactalbumin by chymosin and pepsin. Effect of conformation and pH

Miranda, Guy; Haze, G.; Scanff, P.; Pélissier, J.P.

doi:10.1051/lait:1989630

Cited by 29 publications

(12 citation statements)

References 15 publications

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“…At this time point, the pH of the digesta for unheated and heated WPI were about 3.05 and 2.51, respectively. This probably occurred because when the pH of digestion is lower than 4.0, α-LA and β-LG are more accessible to hydrolysis by pepsin (Miranda et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

Gastric digestion of milk protein ingredients: Study using an in vitro dynamic model

Wang

Lin

et al. 2018

Journal of Dairy Science

117

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The coagulation behavior and the kinetics of protein hydrolysis of skim milk powder, milk protein concentrate (MPC), calcium-depleted MPC, sodium caseinate, whey protein isolate (WPI), and heated (90°C, 20 min) WPI under gastric conditions were examined using an advanced dynamic digestion model (i.e., a human gastric simulator). During gastric digestion, these protein ingredients exhibited various pH profiles as a function of the digestion time. Skim milk powder and MPC, which contained casein micelles, formed cohesive, ball-like curds with a dense structure after 10 min of digestion; these curds did not disintegrate over 220 min of digestion. Partly calcium-depleted MPC and sodium caseinate, which lacked an intact casein micellar structure, formed curds at approximately 40 min, and a loose, fragmented curd structure was observed after 220 min of digestion. In contrast, no curds were formed in either WPI or heated WPI after 220 min of digestion. In addition, the hydrolysis rates and the compositions of the digesta released from the human gastric simulator were different for the various protein ingredients, as detected by sodium dodecyl sulfate-PAGE. Skim milk powder and MPC exhibited slower hydrolysis rates than calcium-depleted MPC and sodium caseinate. The most rapid hydrolysis occurred in the WPI (with and without heating). This was attributed to the formation of different structured curds under gastric conditions. The results offer novel insights about the coagulation kinetics of proteins from different milk protein ingredients, highlighting the critical role of the food matrix in affecting the course of protein digestion.

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Section: Discussionmentioning

confidence: 99%

Gastric digestion of milk protein ingredients: Study using an in vitro dynamic model

Wang

Lin

et al. 2018

Journal of Dairy Science

117

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“…The conformational state of a protein is known to affect its rate of proteolysis (10,11). Native globular proteins assume a conformational state which may render them somewhat resistant to proteolysis.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Hydrolysis of Heat-Induced Aggregates of Whey Protein Isolate

O’Loughlin

Murray

Kelly

et al. 2012

J. Agric. Food Chem.

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The effects of heat induced denaturation and subsequent aggregation of Whey Protein Isolate (WPI) solutions on the rate of enzymatic hydrolysis was investigated.Denaturation of whey proteins was monitored by reversed-phase and size exclusion HPLC and observed by native-and SDS-PAGE. Treated and un-treated WPI solutions (100 g L -1 protein) were hydrolysed to a target degree of hydrolysis (DH) of 5 % with Corolase ® PP. Aggregate formation was monitored using light microscopy, with size distribution determined by particle size. Viscosity and surface hydrophobicity exhibited large increases with heat-treatment and the major protein components in WPI showed differences in their rates of aggregation. Results revealed an increased rate of hydrolysis of protein solutions, which were subjected to a pre-hydrolysis heat-

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“…According to Miranda et al . (1989), bovine chymosin can hydrolyse only 10% of α‐La under nonacidic conditions (pH < 4). Meanwhile, the bromelain protease hydrolysed to some extent both whey proteins (Figure 4).…”

Section: Resultsmentioning

confidence: 99%

“…The bovine chymosin and the recombinant camel chymosin had a mild effect on α-La and did not hydrolyse the β-Lg (Figure 4). According to Miranda et al (1989), bovine chymosin can hydrolyse only 10% of α-La under nonacidic conditions (pH < 4). Meanwhile, the bromelain protease hydrolysed to some extent both whey proteins (Figure 4).…”

Section: Proteolysis On Milk Gelsmentioning

confidence: 99%

The impact of chymosin and plant‐derived proteases on the acid‐induced gelation of milk

Beltrán‐Espinoza

Domínguez‐Lujan

Gutiérrez‐Méndez

et al. 2021

Int J of Dairy Tech

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This work aimed to study milk gel formation during a slow fermentation process and the simultaneous action of different proteases like bovine chymosin, recombinant camel chymosin, ficin and bromelain. The acid-induced gels with bovine chymosin and recombinant camel chymosin were firmer than the control gels without proteases or the gels added with plant proteases. However, the acid-induced gels with chymosins had a considerable water release and shrunk in volume as the milk fermentation progressed. In contrast, the acid-induced gels added with bromelain and ficin were softer and showed less syneresis, even at acidic pHs.

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Hydrolysis of α-lactalbumin by chymosin and pepsin. Effect of conformation and pH

Cited by 29 publications

References 15 publications

Gastric digestion of milk protein ingredients: Study using an in vitro dynamic model

Gastric digestion of milk protein ingredients: Study using an in vitro dynamic model

Enzymatic Hydrolysis of Heat-Induced Aggregates of Whey Protein Isolate

The impact of chymosin and plant‐derived proteases on the acid‐induced gelation of milk

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