Kinetic characterization of hydrolysis of camel and bovine milk proteins by pancreatic enzymes

Salami, Maryam; Yousefi, Reza; Ehsani, Mohammad Reza; Dalgalarrondo, Michèle; Chobert, Jean‐Marc; Haertlé, Thomas; Razavi, Seyed Hadi; Saboury, Ali Akbar; Niasari-Naslaji, Amir; Moosavi-Movahedi, Ali Akbar

doi:10.1016/j.idairyj.2008.06.003

Cited by 85 publications

(56 citation statements)

References 28 publications

(23 reference statements)

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“…It shows direct comparison of the effectiveness of enzyme towards different substrates (Bisswanger 2004;Salami et al 2008). Based on kinetic parameter results (Table 3), thermolysin and proteinase K revealed higher K cat /K m ratio when sarcoplasmic protein was used as substrate than myofibrillar protein.…”

Section: Sds-page Analysismentioning

confidence: 97%

“…Higher K m means enzyme needs higher concentration of substrate with lower affinity toward substrate in an enzymatic reaction (Shargel et al 2005;Taylor and DiersCaviness 2003). To measure kinetic parameters of hydrolysis (a) (b) (Salami et al 2008) were plotted reciprocally (Linweaver-Burk plot). In this study both enzymes when acting on peptide bonds of sarcoplasmic and myofibrillar protein showed MichaelisMenton behavior (R>0.97) (Fig.…”

Section: Sds-page Analysismentioning

confidence: 99%

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Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

et al. 2011

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This study was conducted to evaluate the kinetic characteristics of proteolytic activity of proteases on Channa striatus protein fractions. Degree of hydrolysis (DH), amino acid composition and kinetic parameters of sarcoplasmic and myofibrillar proteins were investigated when incubated with proteinase K and thermolysin, separately. After 30 min incubation with proteases, a decrease in DH of sarcoplasmic protein was observed whereas, hydrolysis of myofibrillar protein with proteases took 2 h with an increase in DH. The major amino acids were glutamic acid (16.6%) in thermolysin-myofibrillar hydrolysate followed by aspartic acid (11.1%) in sarcoplasmic protein fraction with no enzyme treatment and lysine (10%) in thermolysinmyofibrillar hydrolysate. The apparent Michaelis constant of proteinase K was lower than thermolysin for both sarcoplasmic and myofibrillar proteins. However, rate of turnover and enzyme efficiency suggested that sarcoplasmic and myofibrillar proteins are suitable substrates for proteinase K and thermolysin hydrolytic reaction, respectively.

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Section: Sds-page Analysismentioning

confidence: 97%

Section: Sds-page Analysismentioning

confidence: 99%

Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

et al. 2011

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“…However, the extent of proteolysis depends on protease accessibility to peptide bonds as well as to the hydrolytic conditions (SALAMI et al, 2008).…”

Section: Antioxidant Activity Evaluation Of Caprine Casein Hydrolysatesmentioning

confidence: 99%

Biotechnological richness of the northeastern semi-arid region: antioxidant activity of casein hydrolysates from Moxotó goat milk (Capra hircus Linnaeus, 1758) obtained by papain action

et al. 2013

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“…At least, some portion of β-CN of both species treated by trypsin or chymotrypsin remained uncleaved even after 15 min of digestion. It seems that this protein, which contains four phosphoseryl residues, could better resist digestion by trypsin or chymotrypsin than bovine α S1 -CN containing eight phosphate groups (Salami et al, 2008). Thus, another factor must be taken into account to explain the greater hydrolysis of α S1 -CN by trypsin, chymotrypsin or papain compared with β-CN, which could be the number of target peptide bonds available for attack by the proteases.…”

Section: Enzymatic Hydrolysis Of Whole Camel Caseinmentioning

confidence: 99%

Separation and characterization of major milk proteins from Algerian<br>Dromedary (Camelus dromedarius)

Saliha

Dalila

Chahra

et al. 2013

Emir. J. Food Agric

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To characterize major protein fraction in Algerian dromedary's milk, two samples from Sahraoui population collected from two different regions were analyzed using electrophoretic and chromatographic techniques. Casein components and whey proteins were separated by DEAE-cellulose ion exchange chromatography and Sephacryl S200 permeation gel chromatography respectively, and then identified by polyacrylamide gel electrophoresis which looked different from the corresponding patterns of the caseins and whey proteins from cow milk. Differences in casein composition between camel and bovine milk may influence their digestibility, hydrolysis of camel milk caseins using four different proteases (trypsin, chymotrypsin, pepsin and papain) was studied. Caseins were more rapidly hydrolyzed by pepsin because of the greater number of potential pepsin cleavage sites present in the primary structures of camel caseins.

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Kinetic characterization of hydrolysis of camel and bovine milk proteins by pancreatic enzymes

Cited by 85 publications

References 28 publications

Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

Kinetic characterization of Channa striatus muscle sarcoplasmic and myofibrillar protein hydrolysates

Biotechnological richness of the northeastern semi-arid region: antioxidant activity of casein hydrolysates from Moxotó goat milk (Capra hircus Linnaeus, 1758) obtained by papain action

Separation and characterization of major milk proteins from Algerian<br>Dromedary (Camelus dromedarius)

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