Nomenclature of the Proteins of Cows’ Milk—Sixth Revision

The principal pathways for the formation of flavour compounds in cheese (glycolysis, lipolysis and proteolysis) are reviewed. Depending on variety, microflora and ripening conditions, lac- tate may be metabolized by a number of pathways to various compounds which contribute to cheese flavour or off-flavours. Citrate metabolism by citrate-positive lactococci or Leuconostoc spp. is important in certain varieties (e.g., Dutch cheeses). Lipolysis results directly in the formation of flavour compounds by liberating free fatty acids (FFA). FFA may also be metabolized to alkan-2-ones and fatty acid lactones. Proteolysis of the caseins to a range of small- and intermediate-sized peptides and free amino acids (FAA) probably only contributes to the background flavour of most cheese varieties, but FAA are important precursors for a range of poorly-understood catabolic reactions which produce volatile compounds essential for flavour.

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Biochemical pathways for the production of flavour compounds in cheeses during ripening: A review

Rennet-coagulated cheeses are ripened for periods ranging from about two weeks to two or more years depending on variety. During ripening, microbiological and biochemical changes occur that result in the development of the flavour and texture characteristic of the variety. Biochemical changes in cheese during ripening may be grouped into primary (lipolysis, proteolysis and metabolism of residual lactose and of lactate and citrate) or secondary (metabolism of fatty acids and of amino acids) events. Residual lactose is metabolized rapidly to lactate during the early stages of ripening. Lactate is an important precursor for a series of reactions including racemization, oxidation or microbial metabolism. Citrate metabolism is of great importance in certain varieties. Lipolysis in cheese is catalysed by lipases from various source, particularly the milk and cheese microflora, and, in varieties where this coagulant is used, by enzymes from rennet paste. Proteolysis is the most complex biochemical event that occurs during ripening and is catalysed by enzymes from residual coagulant, the milk (particularly plasmin) and proteinases and peptidases from lactic acid bacteria and, in certain varieties, other microorganisms that are encouraged to grow in or on the cheese. Secondary reactions lead to the production of volatile flavour compounds and pathways for the production of flavour compounds from fatty acids and amino acids are also reviewed.

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Biochemistry of Cheese Ripening

Nomenclature of Proteins of Cow's Milk: Fifth Revision

Dipeptidyl-peptidase IV/CD26 (DPP IV) is a cell-surface protease belonging to the prolyloligopeptidase family. It selectively removes the N-terminal dipeptide from peptides with proline or alanine in the second position. Apart from its catalytic activity, it interacts with several proteins, for instance, adenosine deaminase, the HIV gp120 protein, fibronectin, collagen, the chemokine receptor CXCR4, and the tyrosine phosphatase CD45. DPP IV is expressed on a specific set of T lymphocytes, where it is up-regulated after activation. It is also expressed in a variety of tissues, primarily on endothelial and epithelial cells. A soluble form is present in plasma and other body fluids. DPP IV has been proposed as a diagnostic or prognostic marker for various tumors, hematological malignancies, immunological, inflammatory, psychoneuroendocrine disorders, and viral infections. DPP IV truncates many bioactive peptides of medical importance. It plays a role in glucose homeostasis through proteolytic inactivation of...

Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV.

/pdf/etude-du-role-des-micro-organismes-et-des-enzymes-au-cours-4gmx9nt0gw.pdf

Etude du rôle des micro-organismes et des enzymes au cours de la maturation des fromages. II. - Influence de la présure commerciale

Adding α-Ketoglutarate to Semi-hard Cheese Curd Highly Enhances the Conversion of Amino acids to Aroma Compounds

Autolysis of two strains of Lactococcus lactis during cheese ripening

Lactococcus lactis subsp. lactis NCDO 763 (also designated ML3) possesses an X-prolyl dipeptidyl aminopeptidase (X-PDAP; EC 3.4.14.5). X-PDAP mutants were selected by an enzymatic plate assay on the basis of their inability to hydrolyze an L-phenylalanyl-L-proline-beta-naphthylamide substrate. A DNA bank from L. lactis subsp. lactis NCDO 763 was constructed in one of these X-PDAP mutants, and one clone in which the original X-PDAP phenotype was restored was detected by the enzymatic plate assay. The X-PDAP gene, designated pepXP, was further subcloned and sequenced. It codes for a protein containing 763 residues. Comparison of the amino-terminal sequence of the X-PDAP enzyme with the amino acid sequence deduced from the pepXP gene indicated that the enzyme is not subjected to posttranslational modification or exported via processing of a signal peptide. The pepXP gene from L. lactis subsp. lactis NCDO 763 in more than 99% homologous to the pepXP gene from L. lactis subsp. cremoris P8-2-47 described elsewhere (B. Mayo, J. Kok, K. Venema, W. Bockelmann, M. Teuber, H. Reinke, and G. Venema, Appl. Environ. Microbiol. 57:38-44, 1991) and is also conserved in other lactococcal strains.

Cloning and DNA sequence analysis of an X-prolyl dipeptidyl aminopeptidase gene from Lactococcus lactis subsp. lactis NCDO 763.

An X-prolyl dipeptidyl peptidase (EC 3.4.14.5) has been purified from a crude intracellular extract from Lactococcus lactis spp. lactis NCDO 763 by ion-exchange chromatography and gel filtration. One protein band was detected after electrophoresis of the purified enzyme in the presence or absence of sodium dodecyl sulphate. The enzyme is a 190 kDa dimer composed of identical subunits. Optimal activity occurs at pH 8.5 and 40–45°C and the enzyme is inhibited by reagents specific for serine proteases, such as diisopropylfluorophosphate. The enzyme hydrolyzes p-nitroanilide- or β-naphthylamide-substituted X-Pro dipeptides, as well as β-casomorphin.

Jean-Claude Gripon

Papers

Etude du rôle des micro-organismes et des enzymes au cours de la maturation des fromages. II. - Influence de la présure commerciale

Adding α-Ketoglutarate to Semi-hard Cheese Curd Highly Enhances the Conversion of Amino acids to Aroma Compounds

Autolysis of two strains of Lactococcus lactis during cheese ripening

Cloning and DNA sequence analysis of an X-prolyl dipeptidyl aminopeptidase gene from Lactococcus lactis subsp. lactis NCDO 763.

Intracellular X-prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis: purification and properties