Influence of chymosin type and curd scalding temperature on proteolysis of hard cooked cheeses

Costabel, Luciana María; Bergamini, Carina Viviana; Pozza, Leila; Cuffia, Facundo; Candioti, Mario César; Hynes, Erica Rut

doi:10.1017/s0022029915000175

Cited by 17 publications

(10 citation statements)

References 45 publications

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“…Residual coagulant activity in cheese samples was analyzed using the method described in Costabel et al (2015). The activity was expressed as the nanomoles of product [tripeptide (NO 2 -Phe)-Arg-Leu] released by coagulant per hour per gram of dried minicurd.…”

Section: Residual Coagulant Activitymentioning

confidence: 99%

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Plasmin and coagulant activities in a minicurd model system: Study of technological parameters

Vélez

Perotti

Candioti

et al. 2016

Journal of Dairy Science

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The effect of scalding temperature of the curd, the inclusion of a washing step, and the pH at whey drainage on plasmin and coagulant activities were assessed in a minicurd model of young hard cooked cheese. The variables were tested as follows: draining pH was assayed at 3 levels (4.6, 5.6, and 6.4), curd scalding temperature was tested at 50 and 56°C, and washing of the curd was examined at 2 levels (no washing step, and the replacement of the whey by water). Increase in pH at whey drainage and washing of the curd had a positive effect on plasmin activity, which was also evidenced by compatible changes in soluble peptide profiles. No effect of increased cooking temperature was found on plasmin activity. Plasminogen activation was not verified in any treatment. As for coagulant, lower pH values at whey drainage and a decrease in curd cooking temperature increased its activity; washing of the curd showed no influence on coagulant residual activity. These results were consistent with proteolysis described by peptide profiles, electrophoresis, and soluble nitrogen fractions.

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Section: Residual Coagulant Activitymentioning

confidence: 99%

“…It is known that lower amounts of rennet are retained in hard cheeses due to their lower moisture content, and to the denaturation caused by temperature. Despite these facts, inactivation of the coagulant in cooked cheeses has been reported to be partial or reversible (Hayes et al, 2002;Hynes et al, 2004;Costabel et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Plasmin and coagulant activities in a minicurd model system: Study of technological parameters

Vélez

Perotti

Candioti

et al. 2016

Journal of Dairy Science

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“…An increase in the heating temperature of the clot from 50 to 56 °C when producing very hard, granular, cows' milk cheese using the rChn of a cow or a camel leads to a significant decrease in the concentration of products of proteolysis of αS1-casein. But even after processing the clot at 56 °C, the concentration of markers of proteolysis of αS1-casein was higher in maturing and stored cheeses produced using a more thermally stable rChn-Cam than when using rChn-Bos (Costabel et al, 2015). This is despite the fact that the general PA of a camel enzyme is 3.5-4.0 times than that of a cow (Kappeler al., 2006).…”

Section: Technological Propertiesmentioning

confidence: 99%

Biochemical and technological properties of moose (<i>Alces alces</i>) recombinant chymosin

et al. 2022

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Recombinant chymosins (rСhns) of the cow and the camel are currently considered as standard milk coagulants for cheese-making. The search for a new type of milk-clotting enzymes that may exist in nature and can surpass the existing “cheese-making” standards is an urgent biotechnological task. Within this study, we for the first time constructed an expression vector allowing production of a recombinant analog of moose chymosin in the expression system of Escherichia coli (strain SHuffle express). We built a model of the spatial structure of moose chymosin and compared the topography of positive and negative surface charges with the correspondent structures of cow and camel chymosins. We found that the distribution of charges on the surface of moose chymosin has common features with that of cow and camel chymosins. However, the moose enzyme carries a unique positively charged patch, which is likely to affect its interaction with the substrate. Biochemical and technological properties of the moose rChn were studied. Commercial rСhns of cow and camel were used as comparison enzymes. In some technological parameters, the moose rChn proved to be superior to the reference enzymes. Сompared with the cow and camel rСhns, the moose chymosin specific activity is less dependent on the changes in CaCl2 concentration in the range of 1–5 mM and pH in the range of 6–7, which is an attractive technological property. The total proteolytic activity of the moose rСhn occupies an intermediate position between the rСhns of cow and camel. The combination of biochemical and technological properties of the moose rСhn argues for further study of this enzyme.

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“…For example, for the production of cheeses with a high temperature of the second heating and long periods of maturation and storage, milk coagulants that are stable at temperatures of 50°C or less are in demand. A milk-clotting enzyme with high TC, which remains active after cheese grain is heated to 52-58°C, can exhibit undesirable PA in cheese and worsen its physicochemical and organoleptic parameters [41,42].…”

Section: Lane 8)mentioning

confidence: 99%

Can Recombinant Tree Shrew (Tupaia belangeri chinensis) Chymosin Coagulate Cow (Bos taurus) Milk?

Balabova

Belenkaya²,

Volosnikova³

et al. 2022

Appl Biochem Microbiol

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Genetically engineered chymosin from the tree shrew (Tupaia belangeri chinensis) has been obtained and partially characterized for the first time. The target enzyme was produced in Escherichia coli, strain BL21(DE3). It was shown that tree shrew recombinant chymosin coagulates cow milk (Bos taurus). The total and specific milk-clotting activity of the obtained enzyme was 0.7–5.3 IMCU/mL and 8.8–16.6 IMCU/mg. The nonspecific proteolytic activity of tree shrew recombinant chymosin in relation to total bovine casein was 30 and 117% higher than that of recombinant chymosin of cow and of single-humped camel respectively. It was found that in comparison with most of the known genetically engineered chymosins, the tree shrew enzyme showed exceptionally low thermal stability. After heating at 45°C, the coagulation ability of tree shrew recombinant chymosin decreased by more than 40%, and at 50°C the enzyme lost more than 90% of the initial milk-clotting activity. The Michaelis constant (Km), enzyme turnover number (kcat), and catalytic efficiency (kcat/Km) for genetically engineered chymosin from the tree shrew were 6.3 ± 0.1 µM, 11 927 ± 3169 s–1 and 1968 ± 620 µM–1 s–1, respectively. Comparative analysis showed that the primary structure of the chymosin-sensitive site of cow kappa-casein and the supposed similar sequence of tree shrew kappa-casein differed by 75%. The ability of tree shrew recombinant chymosin to coagulate cow’s milk, along with a low thermal stability and high catalytic efficiency with respect to the substrate, imitating the chymosin-sensitive site of cow kappa-casein, suggests that this enzyme is of potential interest for cheese making.

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Influence of chymosin type and curd scalding temperature on proteolysis of hard cooked cheeses

Cited by 17 publications

References 45 publications

Plasmin and coagulant activities in a minicurd model system: Study of technological parameters

Plasmin and coagulant activities in a minicurd model system: Study of technological parameters

Biochemical and technological properties of moose (<i>Alces alces</i>) recombinant chymosin

Can Recombinant Tree Shrew (Tupaia belangeri chinensis) Chymosin Coagulate Cow (Bos taurus) Milk?

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