Identification of Low Molecular Weight Peptides in Gouda‐type Cheese and Evidence for the Formation of These Peptides from 23 N‐terminal Residues of αsl‐casein by Proteinases of <i>Streptococcus cremoris H61</i>

Kaminogawa, Shuichi; Yan, Tsong‐Rong; Azuma, Norihiro; Yamauchi, Kunio

doi:10.1111/j.1365-2621.1986.tb13098.x

Cited by 56 publications

(27 citation statements)

References 6 publications

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“…meyer, 1974;Visser et al, 1983b). Results obtained by Kaminogawa et al (1986) and Pham and Nakai (1984) have proposed the reversed-phase high-performance liquid chromatography (RP-HPLC) of the water soluble fraction of cheese as a potential tool for a more objective evaluation of ripening of Cheddar cheese.…”

Section: Isolation and Identification Of Bitter Peptidesmentioning

confidence: 99%

Bitter flavour in dairy products. II. A review of bitter peptides from caseins: their formation, isolation and identification, structure masking and inhibition

Lemieux

Simard

1992

Lait

182

116

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Summary -Bitterness, a f1avour defect liable to be present in dairy products, is due to the accumulation of bitter-tasting peptides. These peptides are rich in hydrophobie amino acids and are formed by the action of proteolytic enzymes on casein. Many studies report the isolation, identification, and characterisation of bitter peptides from cheese and casein hydrolysates, and even their synthesis. This has been done in arder ta determine the structure of peptides, and also to elucidate the roles of different proteolytic enzyme systems in the development of bitterness, the exact nature of which is still hypothetical. Although bitterness has to be accepted as a necessary consequence of proteolysis, it can be mitigated by masking, removal, or prevention.bitterness 1 cheese 1 casein hydrolysate 1 peptide 1 hydrophobicity Résumé -L'amertume dans les produits laitiers. Il. Une revue de la littérature sur la nature des peptides amers issus de la protéolyse des caséines et concernant leur formation, isolement, identification, structure, camouflage et inhibition.

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Section: Isolation and Identification Of Bitter Peptidesmentioning

confidence: 99%

Bitter flavour in dairy products. II. A review of bitter peptides from caseins: their formation, isolation and identification, structure masking and inhibition

Lemieux

Simard

1992

Lait

182

116

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“…The purpose of this study and another study (10) was to identify and characterize an L. helveticus endopeptidase(s) involved in the hydrolysis of ␤-CN(f193-209). Additionally, the accumulation of ␣ s1 -CN(f1-9) has been associated with bitterness (4,5,15); therefore, the hydrolysis of this peptide was also examined.…”

mentioning

confidence: 99%

Identification and Characterization of Lactobacillus helveticus PepO2, an Endopeptidase with Post-Proline Specificity

Chen¹,

Christensen

Broadbent

et al. 2003

Appl Environ Microbiol

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A post-proline endopeptidase (PepO2) was detected in cell extracts from a genomic library of Lactobacillus helveticus CNRZ32 by using the synthetic substrate N-acetyl-␤-casein-(f203-209)--nitroanilide in a coupled reaction with aminopeptidase N. Isolates with activity for this substrate contained plasmids with visually indistinguishable restriction profiles. Nucleotide sequence analysis revealed a 1,947-bp open reading frame, designated pepO2, encoding a putative 71.4-kDa protein. Analysis of the predicted peptide sequence revealed that L. helveticus PepO2 contained the zinc-dependent metalloprotease motif HEXXH and exhibited levels of amino acid sequence similarity of 72, 61, 59, and 53% to L. helveticus PepO, Lactococcus lactis PepO2, L. lactis PepO, and Lactobacillus rhamnosus PepO, respectively. Northern hybridization results indicated that the transcript containing pepO2 was monocistronic. Despite the high degrees of amino acid similarity to PepO proteins from other lactic acid bacteria, the specificity of the L. helveticus PepO2 for post-proline bonds distinguishes it from other PepO-type endopeptidases characterized to date. The specificity for post-proline bonds also suggests that this enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as ␤-casein(f193-209).The proteolytic systems of dairy lactic acid bacteria (LAB) have received extensive research attention due to their importance in the physiology of these organisms and in cheese flavor development. LAB are fastidious microorganisms with multiple amino acid auxotrophies (18). During growth in milk, LAB rely on their proteolytic systems to obtain essential amino acids from caseins (CNs), the most abundant proteins in milk (9, 17). Additionally, proteolytic enzymes from LAB produce flavor compounds and precursors that are essential for cheese flavor development (9, 23).The proteolytic systems of LAB can be functionally divided into three components: (i) cell envelope-associated proteinases which hydrolyze CNs to oligopeptides; (ii) peptide transport systems, of which the oligopeptide transport system is the most important in milk and cheese; and (iii) numerous intracellular peptidases (9, 17). The intracellular peptidases of LAB include both endopeptidases and aminopeptidases. Endopeptidases, due to their ability to hydrolyze peptide bonds within a peptide, are of particular interest in targeting peptides for rapid hydrolysis. In Lactococcus lactis, the best-characterized LAB, the endopeptidases that have been identified include PepO, PepO2, PepF1, and PepF2. All of these enzymes are metalloproteases, and PepO, PepF1, and PepF2 are encoded in operons (9, 17). The physiological roles of these endopeptidases remain unclear; however, PepF appears to be important for protein turnover during nitrogen starvation (24). To date, one metalloendopeptidase, designated PepO (8), and a thiol-dependent endopeptidase, designated PepE (13), have been characterized from Lactobacillus helveticus.The ability of L. helveticus CNRZ32 to ...

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“…The N-terminal sequence of these peptides is Arg.Pro.Lys.His.Pro ... and should be hydrolysed by PepX. The fact that they accumulate in Cheddar [and in Gouda (Kaminogawa et al, 1986;Exterkate and Alting, 1995)] suggests that either PepX is unstable or inactive in cheese or that it is unable to hydrolyse the above sequence, perhaps due to its high positive charge. The smaller peptides are difficult to isolate and especially to sequence (they do not adsorb on the membrane of the sequencer); we are now focussing attention on these small peptides.…”

Section: Characterization Of Proteolysis In Cheesementioning

confidence: 97%

Rennets: their role in milk coagulation and cheese ripening

Fox¹,

McSweeney²

1997

Microbiology and Biochemistry of Cheese and Fermented Milk

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Identification of Low Molecular Weight Peptides in Gouda‐type Cheese and Evidence for the Formation of These Peptides from 23 N‐terminal Residues of αsl‐casein by Proteinases of Streptococcus cremoris H61

Cited by 56 publications

References 6 publications

Bitter flavour in dairy products. II. A review of bitter peptides from caseins: their formation, isolation and identification, structure masking and inhibition

Bitter flavour in dairy products. II. A review of bitter peptides from caseins: their formation, isolation and identification, structure masking and inhibition

Identification and Characterization of Lactobacillus helveticus PepO2, an Endopeptidase with Post-Proline Specificity

Rennets: their role in milk coagulation and cheese ripening

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