Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid

Adler‐Nissen, Jens

doi:10.1021/jf60226a042

Cited by 1,381 publications

(746 citation statements)

References 9 publications

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“…The degree of hydrolysis (DH) was calculated by the determination of free amino group after the reaction with 2, 4, 6-trinitrobenzenesulfonic acid (TNBS) following the method described by Adler-Nissen (1979) with slight modification. About 0.25 ml of protein hydrolysate was withdrawn after the hydrolysis reaction into 2.0 ml of aqueous 1 % SDS and incubated at 70°C for 15 min.…”

Section: Degree Of Hydrolysismentioning

confidence: 99%

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

et al. 2015

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A low molecular weight type-II collagenous polypeptide (CIIp) from whale shark (WS) cartilage was prepared by thermolysin digestion; and examined for their physico-functional and antioxidant properties. The purified collagen was composed of an identical (α 1 ) 3 chains and was characterized as type-II. After hydrolysis with thermolysin, the α-chain of the WS collagen was degraded into smaller peptides with molecular weight ranging from 70 to 20KDa. CIIp was successfully separated from the hydrolysates with molecular weight of approximately 37 kDa. Amino acid analysis of CII, and CIIp indicated imino acid contents of 155 and 121 amino acid residues per 1000 residues, respectively. Differing Fourier transform infrared (FTIR) spectra of CII and CIIp were observed, which suggested that the hydrolysis process by thermolysin affected the secondary structure and molecular order of collagen, particularly the triple-helical structure. The denaturation temperature of CII (34°C) was higher than that of CIIp. Low content of glycoprotein was observed in CII than CIIp due to removal of some polypeptides by thermolysin digestion. The antioxidant activity against 1,1-diphenyl-2-picrylhydrazyl radicals and the reducing power of CIIp was greater than that of CII. The results proposed that the purified CIIp from WS cartilage with excellent antioxidant activities could be the suitable biomaterial for therapeutic applications.

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Section: Degree Of Hydrolysismentioning

confidence: 99%

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

et al. 2015

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“…Where, h is the number of broken peptide bonds per unit weight, and h tot is the total number of bonds per unit weight and equals 8.2 meq⋅g −1 proteins for casein (Adler-Nissen 1979).…”

Section: Analysis Of Protease Activity and Protein Or Peptide Contentmentioning

confidence: 99%

Optimization of some conditions of Neutrase-catalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase

Kong

Zhao

2011

J Food Sci Technol

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Casein hydrolysate was prepared by hydrolyzing casein with Neutrase and then modified by a Neutrasecatalyzed plastein reaction. The prepared hydrolysate had a degree of hydrolysis of 13.0% and exhibited ACE inhibition in vitro with an IC 50 value of 40.4 μg⋅mL −1 . With the decreased amount of free amino groups of the modified hydrolysate as the response, some conditions of the plastein reaction including substrate concentration, enzyme to substrate ratio, reaction temperature and time were studied by single factor experiments and response surface methodology, and optimized finally as 62% (w/w), 3.0 kU⋅g −1 peptides, 30°C and 6.3 h, respectively. The maximum decreased amount of free amino groups of the modified hydrolysate prepared under these optimized conditions was 210.0 μmol⋅g −1 peptides, while corresponding IC 50 value was lowered to 14.7 μg⋅mL −1 . The present result indicates that Neutrase-catalyzed plastein reaction was capable of enhancing ACE-inhibitory activity in vitro of casein hydrolysate, and also highlights the importance of a forthcoming study to investigate the peptide compositions of the modified hydrolysate and the role of protease used in the plastein reaction.

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“…These results suggest that haem iron uptake by intestinal cells could be affected by two phenomena: the haem state and the strength of the haem-peptide interaction in hydrolysate solutions. At pH 10 haemoglobin in its native form is hydrolysed by subtilisin via a 'one-by-one' mechanism (Adler-Nissen, 1979). Haemoglobin releases low molecular weight peptides throughout the reaction.…”

Section: Discussionmentioning

confidence: 99%

“…At higher DH, the concentration of these species was not sufficient and haem was solubilised by small peptides which could not prevent its polymerisation. At pH 3, haemoglobin in its denatured form is hydrolysed by pepsin via a 'zipper' mechanism (Adler-Nissen, 1979). Pepsin hydrolysis produced a fairly continuous distribution of intermediate size peptides, which were degraded to small peptides.…”

Section: Discussionmentioning

confidence: 99%

Influence of the extent of haemoglobin hydrolysis on the digestive absorption of haem iron in the rat. An in vitro study

Vaghefi¹,

Nedjaoum²,

Guillochon³

et al. 2000

Exp. Physiol.

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Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid

Cited by 1,381 publications

References 9 publications

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

Optimization of some conditions of Neutrase-catalyzed plastein reaction to mediate ACE-inhibitory activity in vitro of casein hydrolysate prepared by Neutrase

Influence of the extent of haemoglobin hydrolysis on the digestive absorption of haem iron in the rat. An in vitro study

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