Milk coagulants

Green, Margaret L.

doi:10.1017/s0022029900020082

Cited by 104 publications

(10 citation statements)

References 130 publications

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“…The available methods to distinguish chymosin and bovine pepsin A have been reviewed (Green, 1977). The chromatographic method of Garnot et al (1972) which permits active chymosin and bovine pepsin A to be quantified separately offers a simple method for the determination of the absolute activity of each enzyme.…”

mentioning

confidence: 99%

Evaluation of bovine rennets in terms of absolute concentrations of chymosin and pepsin A

Martin

Collin

Garnot

et al. 1981

Journal of Dairy Research

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A method for determining chymosin and bovine pepsin A in commercial extracts of bovine veils, based on the use of the synthetic hexapeptide (LeuSer-Phe(NO 2 )-Nle-Ala-Leu-OMe) as reference substrate, is reported. Chymosin and bovine pepsin A were separated chromatographically from extracts and assayed for clotting activity on a reconstituted skim-milk standardized with reference chymosin and bovine pepsin A, themselves standardized in relation to the hexapeptide. The effect of pH on the absorbance difference between the hexapeptide and the LeuSer-Phe(NO 2 ) tripeptide resulting from its hydrolysis was studied. It was found that the ' optimal' pH for determining the activities of the reference enzyme solutions was 4-7.Six chymosin and 3 bovine pepsin A preparations were assayed on the hexapeptide to define the relation between the proteolytic activity and the amount of active enzyme. At pH 4-7 and 30 °C 1 mg chymosin and 1 mg bovine pepsin A hydrolysed 100 and 2700 /ai-peptide/s respectively. The clotting activity of these preparations was assayed on a reconstituted skim-milk to standardize it and thus define the relation between the clotting time and the amount of active enzyme. Chymosin had a specific clotting activity twice that of bovine pepsin A. At equal clotting activities, bovine pepsin A was 55 times more active than chymosin on the hexapeptide at pH 4-7.

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confidence: 99%

Evaluation of bovine rennets in terms of absolute concentrations of chymosin and pepsin A

Martin

Collin

Garnot

et al. 1981

Journal of Dairy Research

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“…Cheese whey, or milk whey (from now on, simply whey), is the yellowish residual liquid remaining after casein is precipitated out from milk using enzymes or acids (Green, 1977). Whey can then be considered as an aqueous solution of lactose containing mineral salts and some residual protein.…”

Section: Whey As Raw Materials For Upgradingmentioning

confidence: 99%

Whey upgrading by enzyme biocatalysis

Illanes¹

2011

Electro Journal of Biotech

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Whey is a co-product of processes for the production of cheese and casein that retains most of the lactose content in milk. World production of whey is estimated around 200 million tons per year with an increase rate of about 2%/per year. Milk production is seasonal, so surplus whey is unavoidable. Traditionally, whey producers have considered it as a nuisance and strategies of whey handling have been mostly oriented to their more convenient disposal. This vision has been steadily evolving because of the upgrading potential of whey major components (lactose and whey proteins), but also because of more stringent regulations of waste disposal. Only the big cheese manufacturing companies are in the position of implementing technologies for their recovery and upgrading, so there is a major challenge in incorporating medium and small size producers to a platform of whey utilization, conciliating industrial interest with environmental protection within the framework of sustainable development. Within this context, among the many technological options for whey upgrading, transformation of whey components by enzyme biocatalysis appears as prominent. In fact, enzymes are green catalysts that can perform a myriad of transformation reactions under mild conditions and with strict specificity, so reducing production costs and environmental burden. This review pretends to highlight the impact of biocatalysis within a platform of whey upgrading. Technological options are shortly reviewed and then an in-depth and critical appraisal of enzyme technologies for whey upgrading is presented, with a special focus on newly developed enzymatic processes of organic synthesis, where the added value is high, being then a powerful driving force for industrial implementation.

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“…In the food processing industry, proteolysis of milk leading to curd formation is the basis of cheese production. In the manufacture of this food product the firmness of the curd produced following proteolysis of K-casein is a very important consideration, since cutting the curd at the correct firmness ensures that the whey drains properly whilst minimizing the loss of milk solids (Green, 1977). The importance of the casein phosphoserine residues to proper curd formation is indicated by the fact that curd tension was shown to decrease as more of the phosphate groups were removed from the caseins (Reimerdes & Roggenbuck, 1980;Yun et al 19826).…”

Section: Technological Importance Of Casein Phosphorylationmentioning

confidence: 99%

Structure and function of the phosphorylated residues of casein

West

1986

Journal of Dairy Research

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Introduction Phosphorylation of the caseins Determination of the position of phosphorylated residues Structure of the kinase recognition sites Limits to the extent of phosphorylation Properties of the casein kinase Importance of the casein phosphoseryl residues to the structure, function and properties of milk CONTENTS PAGE 333 335 335 338 340 342 343 Formation of micelles and binding of calcium Technological importance of casein phosphorylation Biological significance of casein phosphorylation Conclusion References

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Milk coagulants

Cited by 104 publications

References 130 publications

Evaluation of bovine rennets in terms of absolute concentrations of chymosin and pepsin A

Evaluation of bovine rennets in terms of absolute concentrations of chymosin and pepsin A

Whey upgrading by enzyme biocatalysis

Structure and function of the phosphorylated residues of casein

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