Bitter Peptides, Occurrence and Structure

Guigoz, Y.; Solms, J.

doi:10.1093/chemse/2.1.71

Cited by 69 publications

(36 citation statements)

References 32 publications

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“…Dunhill (1965) then introduced the expression "hydrophobicity" for these values (Guigoz and Solms, 1976). The way for a calculation of bitterness was later opened by Ney (1971) who, introducing Tanford values, published the Qhypothesis, which establishes a semiquantitative relationship between the amino acid composition of a peptide and its bitterness.…”

Section: History Of Bitter Taste Evaluationmentioning

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

187

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: History Of Bitter Taste Evaluationmentioning

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

187

116

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“…This problem is more acute at high values of hydrolysis (Guigoz and Solms, 1976). Matoba and Hata (1972) proposed that the bitterness was caused by peptides with high content of hydrophobic amino acids, regardless of their primary structure.…”

Section: Resultsmentioning

confidence: 99%

Optimized Nitrogen Recovery and Non-Bitter Hydrolysates from Porcine Hemoglobin

Guo

Zhao

Cui

et al. 2008

FSTR

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The combined effects of pH, temperature, buffer/substrate ratio, time and enzyme concentration on nitrogen recovery (NR) from porcine hemoglobin, a by-product of industrial abattoirs, with Pancreatin and Flavourzyme® 500MG enzyme mixture were characterized. The effect of hydrolysis variables on NR was described through response surface analysis (RSA). The results showed that pH and time were the most important parameters and that the buffer/substrate ratio had less of an effect on NR. The mathematical model presented an optimum hydrolysis conditions were as follows: temperature, 50.4 ºC; pH, 7.8; buffer/substrate (containing 33.1% protein) ratio (w/w), 1.4:1; time, 15.4h; and enzyme concentration, 2.0g/kg. The predicted NR value was 98.99%, and the actual value obtained was 97.69%. Molecular mass of recovered hydrolysates ranged from >15 kDa to free amino acid (<1 kDa). The admixture of enzyme had specificity for terminal a variety of hydrophobic amino acids which resulted in recovery of non-bitter hydrolysates from porcine hemoglobin.

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“…Ney (1978) found that hydrolysates from casein, potato protein, soya protein, and wheat gluten were bitter only if they contained appreciable amounts of peptides below an apparent molecular weight of 6000 Dalton. Adler-Nissen and Olsen (1979) and Guigoz and Solms (1976) reported that most of the peptides with a bitter taste are from 7 to 27 amino acid residues, which may set the limit as high as from 1000 Dalton to 3000 Dalton. So our results agreed with the above results for the correlation between bitterness and molecular weight distribution of hydrolysates.…”

Section: Resultsmentioning

confidence: 99%

Molecular Weight Distribution of Protein Hydrolysate by the Enzymic Hydrolysis of Weakly Acid-Treated Wheat Gluten

Hong

Lee²,

Lee

2001

FSTR

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For the production of highly soluble HVP (hydrolysed vegetable protein) by enzymic hydrolysis, wheat gluten suspension (6% w/w, protein) was pretreated with weak acid (0.1 N HCl) at 95°C for 1 h to overcome insolubility of the suspension. After treating it for 3 h with alcalase, flavourzyme was added to the wheat gluten hydrolysate and hydrolysis continued for a further 21 h at 50°C. ␣-Amino nitrogen content (AN, mg/ml) and nitrogen solubility index (NSI, %) of the resulting wheat gluten hydrolysate product was 2.87 mg/ml and 94.9%, respectively. The wheat gluten hydrolysate product contained peptides and free amino acids with molecular weights below 300 dalton. Non-acid treated SPI (soy protein isolate) was also adopted as a protein substrate. The AN and NSI of the resulting SPI hydrolysate were 2.02 mg/ml and 70.4%, respectively. SPI hydrolysate contained proteins and peptides with molecular weights above 80 Dalton and below 7300 Dalton.Keywords: protein hydrolysate, wheat gluten, SPI, enzymic hydrolysis By partial hydrolysis of proteins, characteristics including the functional properties of solubility, foaming capability, emulsion stability and flavouring agent formation can be created or enhanced. Moreover, hydrolysis can be performed to suppress the formation of undesirable and complex odors and colors, as well as to eliminate toxic and anti-nutritional components. The protein hydrolysis is conducted by chemical methods of acid or alkaline treatments and also by various proteolytic enzymes (Lahl & Braun, 1994). For the purposes mentioned above acid hydrolysis can be easily applied in general, but it often causes not only undesirable tastes and odors, but also the loss of essential amino acids, the reaction with non protein substances and the formation of lysinoalanine which limits the use of proteins (Deeslie & Cheryan, 1981, Finley et al., 1982. Acetylation (Franzen & Kinsella, 1976, Kim & Rhee, 1989 and phosphorylation (Kim et al., 1988) treatment of proteins also have some safety problems. Recently in Korea, soy sauce produced by hydrochloric acid treatment has become one of the great social issues due to the formation of the toxic compounds such as MCPD (3-chloro-1,2-propanediol) and DCP(1,3-dichloro-2-propanal) (Velisek et al., 1978, 1980, Rillaer & Beernaert, 1989, Bergen et al., 1992. These can be formed by 5.0-9.5% lipids found in vegetable proteins, such as mono-, di-, triglycerides, phospholipids and glycolipids during reactions with high concentrations of hydrochloric acid at high temperature and long reaction times. Hamm (1992) proposed weak acid pretreatment of wheat gluten and soy protein isolate for the subsequent enzymic hydrolysis to suppress the formation of MCPD and DCP. Recently preferred enzymic hydrolysis of proteins has several difficulties, especially in the process of high protein concentrations and in achieving a high degree of hydrolysis, as well as microbial contamination during long reaction time compared to acid hydrolysis (Lin & Lee, 1987). In order to achieve economic feasib...

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Bitter Peptides, Occurrence and Structure

Abstract: The bitter taste of many protein rich foods resides in the peptide fraction. 61 bitter tasting peptides, isolated from natural systems, and 145 bitter tasting synthetic peptides are reviewed. The relationships between average hydrophobicity and bitter taste are then discussed.

Cited by 69 publications

References 32 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

Optimized Nitrogen Recovery and Non-Bitter Hydrolysates from Porcine Hemoglobin

Molecular Weight Distribution of Protein Hydrolysate by the Enzymic Hydrolysis of Weakly Acid-Treated Wheat Gluten

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