The oligopeptides of sweet and acid cheese whey

Chianese, Lina; Caira, Simonetta; Ferranti, Pasquale; Laezza, P.; Malorni, Antonio; Mucchetti, G.; Garro, Giuseppina; Addeo, Francesco

doi:10.1051/lait:1997650

Cited by 23 publications

(14 citation statements)

References 26 publications

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“…Kindstedt et al (1995) found that proteolysis was significantly slowed down in Mozzarella cheese when a reduced dose of chymosin was used, which indicates that rennet was active during ripening in spite of high cooking temperatures. Other researchers have postulated that α s1 -I is produced by chymosin, but early during cheese making, i.e., before the heating of the curd (Chianese et al, 1996;Gaiaschi et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Influence of Residual Milk-Clotting Enzyme on αs1 Casein Hydrolysis During Ripening of Reggianito Argentino Cheese

Hynes

Aparo

Candioti

2004

Journal of Dairy Science

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Milk-clotting enzyme is considered largely denatured after the cooking step in hard cheeses. Nevertheless, typical hydrolysis products derived from rennet action on alpha(s1)-casein have been detected during the ripening of hard cheeses. The aim of the present work was to investigate the influence of residual milk-clotting enzyme on alpha(s1)-casein hydrolysis in Reggianito cheeses. For that purpose, we studied the influence of cooking temperature (45, 52, and 60 degrees C) on milk-clotting enzyme residual activity and alpha(s1)-casein hydrolysis during ripening. Milk-clotting enzyme residual activity in cheeses was assessed using a chromatographic method, and the hydrolysis of alpha(s1)-casein was determined by electrophoresis and high performance liquid chromatography. Milk-clotting enzyme activity was very low or undetectable in 60 degrees C- and 52 degrees C-cooked cheeses at the beginning of the ripening, but it increased afterwards, particularly in 52 degrees C-cooked cheeses. Cheese curds that were cooked at 45 degrees C had higher initial milk clotting activity, but also in this case, there was a later increase. Hydrolysis of alpha(s1)-casein was detected early in cheeses made at 45 degrees C, and later in those made at higher temperatures. The peptide alpha(s1)-I was not detected in 60 degrees C-cooked cheeses. The results suggest that residual milk-clotting enzyme can contribute to proteolysis during ripening of hard cheeses, because it probably renatures partially after the cooking step. Consequently, the production of peptides derived from alpha(s1)-casein in hard cheeses may be at least, partially due to this proteolytic agent.

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Section: Introductionmentioning

confidence: 99%

Influence of Residual Milk-Clotting Enzyme on αs1 Casein Hydrolysis During Ripening of Reggianito Argentino Cheese

Hynes

Aparo

Candioti

2004

Journal of Dairy Science

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“…Colostrum is rich in nutrients and provides protection against pathogens thanks to its high concentration of antimicrobial proteins and, in particular, immunoglobulins [110,111]. Many milk proteins are precursors of bioactive peptides that are generated by digestive enzymes and during milk fermentation [112].…”

Section: Peptidomics and Nutraceutical Propertiesmentioning

confidence: 99%

Farm animal milk proteomics

Roncada

Piras

Soggiu

et al. 2012

Journal of Proteomics

129

103

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“…Determination of casein hydrolysis. Addeo et al (1992Addeo et al ( , 1994; Alli et al (1998);Chianese et al (1997);Deutsch et al (2000); Fedele et al (1999);Fernandez et al (1998);Ferranti et al (1997); Gagnaire et al (1999Gagnaire et al ( , 2001bGagnaire et al ( , 2004; Gouldsworthy et al (1996); Kunji et al (1998); Marshall & Williams (1988); Molina et al (2002); Roudot-Algaron et al (1994); Shimazaki et al (1988); Singh et al (1999);Trieu-Cuot & Gripon (1981b, 1982; Zappacosta et al (1998);Zeece et al (1989) Gouldsworthy, Leaver, & Banks, 1996;Ferranti et al, 1997;Fernandez, Singh, & Fox, 1998;Alli, Okoniewska, Gibbs, & Konishi, 1998;Singh, Gripon, & Fox, 1999;Gagnaire, Molle´, Herrouin, & Le´onil, 2001b). Peptide identification has allowed the determination of the hydrolytic products resulting from the first steps of degradation of the four main caseins, a s1 -, a s2 -, b-and k-caseins, and has provided information about the main proteolytic agents active in cheese: milk coagulant, milk endogenous and microbial enzymes Singh, Fox, & Healy, 1997;Fernandez et al, 1998;Gagnaire, Boutrou, & Le´onil, 2001a).…”

Section: Proteins Studied Main Applications Proteomic Techniques Refementioning

confidence: 99%