Comparing Proteolytic Action of Milk-Clotting Enzymes on Caseins and Cheese

Mickelsen, R.; Fish, Nancy L.

doi:10.3168/jds.s0022-0302(70)86278-6

Cited by 25 publications

(5 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Table 2 shows the first-order rate constants finally used in the calculation of the curves that best fit the experimental data (Figs 3-5). The overall reaction The initial degradation of /S-casein-B under the influence of rennin action at pH 6-5 is essentially the same as that reported by other workers for /?-casein in whole casein (Fox, 1969a;Ledford, Chen & Nath, 1968;Mickelsen & Fish, 1970). The only major study on the degradation of purified /?-casein has been made by Lindqvist & Storgards (1960), who used free-boundary electrophoresis to investigate the reaction.…”

Section: A Model For the Calculationssupporting

confidence: 80%

The action of rennets on the caseins: I. Rennin action on β-casein-B in solution

Creamer¹,

Mills²,

Richards

1971

Journal of Dairy Research

View full text Add to dashboard Cite

A study of the hydrolysis of /?-casein-B by crystalline rennin or rennet extract at pH 6-5, using a disk electrophoresis technique, showed that 3 bonds in /ff-casein are appreciably more sensitive than the others to rennin proteolysis, and that these bonds are probably located near the C-terminus of the protein. The most susceptible bond is hydrolysed, at 10°C, about 200 times faster than any other bond, whilst at 37 °C it is hydrolysed 60 times faster. A study of the hydrolysis of this bond showed that its rate of hydrolysis at 37°C and pH 6-5 is decreased by either increased ionic strength or increased calcium ion concentration at constant ionic strength. Conformational changes in the substrate are probably responsible for these effects. 270

show abstract

Section: A Model For the Calculationssupporting

confidence: 80%

The action of rennets on the caseins: I. Rennin action on β-casein-B in solution

Creamer¹,

Mills²,

Richards

1971

Journal of Dairy Research

View full text Add to dashboard Cite

show abstract

“…[7][8][9] Proteolytic enzymes of fungal origin have received considerable attention, specially extracellular enzymes of Endothia parasitica, Mucor miehei, and Mucor pusillus, have been received wide acceptability on the industrial scale due to high milk-clotting and low proteolytic activities. [10][11][12][13] Veal rennet or pepsin is very sensitive to milk pH changes, and the high proteolytic activity of trypsin and papain also prevents their use in cheesemaking. 11 Among fungi, an enzyme from Mucor miehei is preferred by the industry to produce milkcoagulation because of its R factor (milk clotting activity/ proteolytic activity), specificity for certain peptide bonds in casein, good cheese quality and yield.…”

Section: Introductionmentioning

confidence: 99%

“…The interaction between macromolecular compounds (proteins, nucleic acids, starch, lignin, etc.) and immobilized biomacromolecules is a quite complex process, with interest in biocatalysis and protein purification. − Calf rennet has been extensively used for cheesemaking all over the world; however, in recent decades due to a shortage of calf rennet on world markets, alternative milk-clotting enzymes of different origins have been investigated. − Proteolytic enzymes of fungal origin have received considerable attention, specially extracellular enzymes of Endothia parasitica , Mucor miehei , and Mucor pusillus , have been received wide acceptability on the industrial scale due to high milk-clotting and low proteolytic activities. − Veal rennet or pepsin is very sensitive to milk pH changes, and the high proteolytic activity of trypsin and papain also prevents their use in cheesemaking . Among fungi, an enzyme from Mucor miehei is preferred by the industry to produce milk-coagulation because of its R factor (milk clotting activity/proteolytic activity), specificity for certain peptide bonds in casein, good cheese quality and yield. ,,− …”

Section: Introductionmentioning

confidence: 99%

Immobilization of Rennet from Mucor miehei via Its Sugar Chain. Its Use in Milk Coagulation

et al. 2004

View full text Add to dashboard Cite

A successful strategy for the immobilization of rennet from Mucor miehei has been developed. The strategy is based on the immobilization of the enzyme, via their sugar chains at high ionic strength on aminated supports having primary amino groups with a very low pK value. The rennet was covalently immobilized via sugar chains (previously oxidized with periodate), which act as natural spacer arms and allow a very high percentage of rennet activity to be kept against small (H-Leu-Ser-p-nitro-Phe-Nle-Ala-Leu-OMe.TFA (98%)) and macromolecular substrates (k-casein) (78%). The use of tailor-made aminated support was critical to obtain good stability values, because using fully aminated supports achieved much lower thermostability values than using 50% aminated supports. The optimized derivative was utilized to hydrolyze casein in milk. To prevent the coagulation of the milk in the presence of the derivative, the reaction was performed at 4 degrees C (where hydrolyzed casein did not precipitate). Then the hydrolyzed milk was filtered and latter on heated to 30 degrees C, achieving a similar aggregate to the one achieved with soluble rennet.

show abstract

“…Although para-K-casein has several potential chymosin cleavage sites, it does not appear to be hydrolysed either in solution or in cheese (Green and Foster, 1974). Mickelsen and Fish (1970) studied the proteinases of C. parasitica and R. pusillus. These enzymes were more proteolytic on various casein substrates (as measured by the liberation of non-protein N) than either pepsin or chymosin.…”

Section: Specificity Of Chymosin and Rennet Substitutes In Cheesementioning

confidence: 99%