Distribution of Milk Clotting Enzymes Between Curd and Whey and Their Survival During Cheddar Cheese Making

Holmes, D.G.; Duersch, J.W.; Ernstrom, C.A.

doi:10.3168/jds.s0022-0302(77)83955-6

Cited by 151 publications

(85 citation statements)

References 16 publications

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“…However, acidification also increases association of the enzyme with the casein molecules [36], and therefore retention of the enzyme in the curd, where its strong activity leads to increased proteolysis [27,51,69,159]. This effect is more significant in rennet-type curds such as Cheddar [69], where acidification in conventional processes essentially follows a fast renneting step and is usually limited, than in soft cheeses where acidification starts prior to rennet addition and largely proceeds throughout the renneting process, curd development and drainage [51]. In Cheddar cheese, acidification of the milk prior to renneting also slows down lactic acid production by the lactic acid bacteria, resulting in inhibited flavour development [11].…”

Section: Technological Means Used To Restore the Cheese-making Propermentioning

confidence: 99%

Formation of heat-induced protein aggregates in milk as a means to recover the whey protein fraction in cheese manufacture, and potential of heat-treating milk at alkaline pH values in order to keep its rennet coagulation properties. A review

Guyomarc’H

2006

Lait

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-The heat-treatment of cheese milk, or whey, to denature the whey proteins has long been the most applied means of recovering these proteins, either directly in the cheese curd, or as added to the cheese milk prior to renneting. In heat-treated milk, the interaction of the denatured whey proteins with the casein micelles, however, limits the primary phase of the enzymatic reaction, and prevents fusion of the casein micelles. Cheeses containing heat-denatured whey proteins also exhibit excessive moisture, a crumbly and soft texture, and poor meltability. Various technological means to reduce these drawbacks are reviewed. Especially, it is generally accepted that the heat-treatment of skim milk at alkaline pH generates aggregates of denatured whey proteins and κ-casein in the serum phase of milk, rather than on the surface of the casein micelles. As a consequence, the casein micelles are depleted in κ-casein, and free of denatured whey proteins. However, the attempts made to exploit this interesting protein distribution in cheese-making remain scarce, despite their promising results. Résumé -Récupération des protéines sériques du lait dans le caillé fromager au moyen de la formation d'agrégats thermo-induits, et intérêt de chauffer le lait à pH alcalin dans le but de conserver son aptitude à la coagulation présure. Revue. Le traitement thermique du lait ou de lactosérum est un des moyens les plus utilisés pour incorporer les protéines sériques ainsi dénatu-rées, soit directement dans le caillé, soit sous forme d'ingrédient ajouté au lait fromager. Cependant, l'interaction entre les protéines sériques dénaturées et les micelles de caséines, due au chauffage du lait, a pour effet de limiter la phase primaire de la coagulation par la présure, ainsi que la fusion des micelles déstabilisées. Les fromages obtenus à partir de lait chauffé sont aussi plus humides, plus mous, plus granuleux et moins aptes à la fonte que les fromages standards. Les moyens technologiques de pallier ces inconvénients sont rappelés. En particulier, il est connu que le traitement thermique du lait à pH alcalin favorise la formation d'agrégats de protéines sériques dénaturées et de caséine κ dans la phase soluble du lait, plutôt qu'en surface des micelles de caséines. En consé-quence, la teneur en caséine κ des micelles est réduite et celles-ci ne sont pas recouvertes de protéi-nes sériques dénaturées. Cependant, peu d'études ont tenté d'exploiter ces caractéristiques du lait chauffé à pH alcalin en technologie fromagère, malgré des résultats prometteurs. coagulation présure / traitement thermique / protéine sérique / fromage

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Section: Technological Means Used To Restore the Cheese-making Propermentioning

confidence: 99%

Formation of heat-induced protein aggregates in milk as a means to recover the whey protein fraction in cheese manufacture, and potential of heat-treating milk at alkaline pH values in order to keep its rennet coagulation properties. A review

Guyomarc’H

2006

Lait

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“…These differences could be due to faster and continued growth of starter culture in MC cheeses during cheddaring and milling compared to SC cheeses, where a pH drop (after a pH of 5.5) was extremely slow (data not shown). This may have an effect on the amount of residual coagulating enzymes in the cheese, which is dependent on the pH of the cheese [8,19]. pH of cheese influences proteolytic changes, which are considered to be the most important biochemical event during the ripening of many cheese varieties.…”

Section: Composition Of Cheesementioning

confidence: 99%

“…Faster proteolysis (Figs. 2 to 5) in MC cheeses could be attributed to their lower pH compared to SC cheeses because of greater residual chymosin activity at lower pH [8,19,25]. It may also be due to the activity of the starter culture, which is known to be proteolytically active during the initial stages of cheese ripening [12].…”

Section: Breakdown Of Casein Fractionsmentioning

confidence: 99%

Melt and rheological properties of Mozzarella cheese as affected by starter culture and coagulating enzymes

Dave

Sharma

McMahon

2003

Lait

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-Low moisture part-skim (LMPS) Mozzarella cheeses were made with single culture (SC) of Streptococcus thermophilus or mixed culture (MC) of Streptococcus thermophilus andLactobacillus helveticus using 1× or 6× of cheese coagulants chymosin or Cryphonectria parasitica (CP). Cheeses were analyzed for total solids, fat, protein, ash, salt, and calcium on day 1. Changes in melt characteristics and proteolysis during storage (4 °C) were monitored on 1, 7, 15, and 30 days (d). After 30 d storage, melt area as measured by modified Schreiber test increased only by approximately 2 times in cheeses made with SC as against 3-4 times in the cheeses made with MC. On d 30, creep test showed that the fall in height decreased by approximately 4-5 times in the SC cheeses but approximately 7-9 times in the cheeses made with MC when compared with the values obtained on d 1 for corresponding cheeses. Melt characteristics on d 7 for cheeses prepared with MC almost corresponded to that of d 30 cheeses made with SC, suggesting faster ripening and increase in melt of cheeses made with MC. Soluble nitrogen was also higher in MC cheeses as compared to those made using SC only. The degradation of total α s -casein was higher in the chymosin cheeses and that of β-casein in the CP cheeses. The degradation of casein fraction f was higher in MC cheeses as compared to those prepared with SC only. After 30 d storage, the highest percentage breakdown of α s -casein was approximately 75% in cheeses made with MC using 6× chymosin and that of β-casein was approximately 50% in cheese samples prepared with MC using 6× coagulant from Cryphonectria parasitica. Meltability of Mozzarella cheese was better correlated to hydrolysis of β-casein and was comparable to soluble nitrogen but least to α s -casein.

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“…Des auteurs ont essayé de quantifier la présure résiduelle dans les caillés : elle serait de l'ordre de 50% en fabrication de Camembert (Vassal et Gripon, 1984) et de 20% en fabrication de Cheddar (Holmes et al, 1977). Son activité au cours de l'affinage varie beaucoup d'un type de fromage à l'autre car les conditions de fabrication jouent un grand rôle dans la rétention et l'activité résiduelle de la présure dans le caillé.…”

Section: Introductionunclassified

Protéolyse et texture des fromages à pâte cuite pressée. II. Influence de la chymosine et des conditions de fabrication

Delacroix-Buchet

Foumier

1992

Lait

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(Reçu le 7 juin 1991; accepté le 25 octobre 1991)Résumé -Au cours de deux séries d'essais, 52 minifromages ont été fabriqués selon une technologique pâte cuite pressée en faisant varier les paramètres technologiques susceptibles de modifier la quantité de chymosine résiduelle et son activité protéolytique dans le fromage en cours d'affinage: pH au soutirage, température de chauffage en cuve, dose.de présure apportée. Deux niveaux de chacun des facteurs ont été étudiés. Un témoin, sans chymosine, coagulé avec Endothia parasitica, a été introduit dans l'essai 2. Les minifromages ont été affinés 40 j et 2 cycles de température d'affinage ont été comparés. Les conditions expérimentales montrent l'évolution de la protéolyse en cours d'affinage. La température d'affinage des fromages a un effet majeur sur la dégradation de la caséine Cls,. La production de la fraction Cls'-I à partir de la caséine Cls, est ralentie par une élévation de la température de chauffage du mélange caillé-sérum en cuve de fabrication de 4 oC, phénomène qui ne peut être attribué que de façon mineure à l'activité de la chymosine.L'augmentation du chauffage en cuve de 4 oC génère, par contre, une accélération de la formation des fractions y à partir de la caséine~liée à "activation du système plasmine-plasminogène.

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Distribution of Milk Clotting Enzymes Between Curd and Whey and Their Survival During Cheddar Cheese Making

Cited by 151 publications

References 16 publications

Formation of heat-induced protein aggregates in milk as a means to recover the whey protein fraction in cheese manufacture, and potential of heat-treating milk at alkaline pH values in order to keep its rennet coagulation properties. A review

Formation of heat-induced protein aggregates in milk as a means to recover the whey protein fraction in cheese manufacture, and potential of heat-treating milk at alkaline pH values in order to keep its rennet coagulation properties. A review

Melt and rheological properties of Mozzarella cheese as affected by starter culture and coagulating enzymes

Protéolyse et texture des fromages à pâte cuite pressée. II. Influence de la chymosine et des conditions de fabrication

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