Kinetic study of the appearance of an anti‐bacterial peptide in the course of bovine haemoglobin peptic hydrolysis

Choisnard, Luc; Froidevaux, Rénato; Nedjar‐Arroume, Naïma; Lignot, Brigitte; Vercaigne-Marko, Dominique; Krier, Francçois; Dhulster, Pascal; Guillochon, Didier

doi:10.1042/ba20010103

Cited by 34 publications

(40 citation statements)

References 28 publications

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“…Choisnard et al [28] reported that during pepsin hydrolysis of protein, one molecule of pepsin cleaved the protein substrate once and then dissociated from it following one-by-one mechanism. In another case, they found one pepsin molecule would cleave the protein substrate multiple times without dissociating from it, thereby generating intermediate peptide products following a zipper mechanism.…”

Section: Hydrolysis Timementioning

confidence: 99%

Extraction of Proteins from Mackerel Fish Processing Waste Using Alcalase Enzyme

Vv¹,

Ae²,

Ms³

et al. 2013

J Bioproces Biotechniq

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Fish proteins are found in the flesh, head, frames, fin, tail, skin and guts of the fish in varying quantities. Unutilized fish and fish processing waste can be used to produce fish proteins which contain amino acids and many bioactive peptides. After removing the fish flesh during the fish processing operation, all other parts are considered wastes which are not properly utilized. The aim of this study was to evaluate the enzymatic extraction of protein from mackerel fish processing waste. Enzymatic extraction of proteins was carried out using alcalase enzyme at three concentrations (0.5, 1 or 2%) and four hydrolysis times (1, 2, 3 and 4 h). The fish protein hydrolysate was dried using a spray dryer to obtain protein powder. The highest protein yield (76.30% from whole fish and 74.53% from the frame) was obtained using 2.0% enzyme concentration after 4 h of hydrolysis. The results showed that increasing the enzyme concentration from 0.5 to 2% (400%) increased the protein yield by 3.13-43.52% depending upon the fish part and reaction time used. Increasing the enzyme concentration by 4 fold for a small increase in protein yield may appear unjustified. Therefore, the enzyme concentration of 0.5% should be used for the protein extraction unless the enzyme is recycled or an immobilized reactor is used in order to reduce the cost associated with the enzyme. Also, increasing the hydrolysis time from 1 to 4 h (400%) increased the protein yield by 16.45 -50.82% depending upon the fish part and enzyme concentration used. Increasing the hydrolysis time by 4 fold for a small increase in protein yield will increase the capital and operating costs of protein production. A shorter hydrolysis time will allow more throughput and/or reduce the volume of the reactor thereby reducing the cost of protein extraction. Therefore, a 1 h reaction time for protein extraction is recommended. The results showed that the combined fish waste can be used for protein extraction without any segregation.

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Section: Hydrolysis Timementioning

confidence: 99%

Extraction of Proteins from Mackerel Fish Processing Waste Using Alcalase Enzyme

Vv¹,

Ae²,

Ms³

et al. 2013

J Bioproces Biotechniq

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“…These ratios were chosen taking into account that in the previous study of hydrolysis of pure synthetic a 1-32 peptide, the ratios were 1/50, 1/100 and 1/200 [17], and that in hemoglobin, there was about ten times more peptide bonds to be hydrolyzed by pepsin than in the pure synthetic a 1-32 peptide [11,14,18].…”

Section: Hydrolysis Proceduresmentioning

confidence: 99%

“…Several studies have investigated the hydrolysis of bovine hemoglobin [11,12,[14][15][16] and numerous antibacterial peptides derived from the hydrolysis of a and b chains of hemoglobin have been identified. These active peptides are classified into four groups: two for a chain and two for b chain.…”

Section: Introductionmentioning

confidence: 99%

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Valorization of cruor slaughterhouse by-product by enzymatic hydrolysis for the production of antibacterial peptides: focus on α 1–32 family peptides mechanism and kinetics modeling

Hedhili

Dimitrov

Vauchel

et al. 2015

Bioprocess Biosyst Eng

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Bovine hemoglobin is the major component of the cruor (slaughterhouse by-product) and can be considered as an important source of active peptides that could be obtained by pepsic hydrolysis. The kinetics of appearance and disappearance of several antibacterial peptides from α 1-32 family during hydrolysis of synthesized α 1-32 peptide, of purified bovine hemoglobin and of cruor was studied, and reaction scheme for the hydrolysis of α 1-32 family peptides from these three sources was determined. On this basis, a mathematical model was proposed to predict the concentration of each peptide of interest of this family depending on hydrolysis time, and also on temperature (in the range 15-37 °C), pH (in the range 3.5-5.5) and enzyme to substrate ratio (in the range 1/50-1/200 for the synthesized peptide and 1/5-1/20 for purified bovine hemoglobin and cruor). Apparent rate constants of reactions were determined by applying the model on a set of experimental data and it was shown that they depended on the temperature according to Arrhenius's law, that their dependence on the pH was linear, and that enzyme to substrate ratio influence was limited (in the studied range).

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“…STC-1 pluri-endocrine cell line was derived from an endocrine tumor developed in the small intestine of double transgenic mice expressing rat insulin promoter for the simian virus 40 large T antigen and the polyoma virus small T antigen [20]. STC-1 cell line is well known for the secretion of CCK phenomenon in intestine.…”

Section: Determination Of the Degree Of Hydrolysis Of Alpha-lactalbuminmentioning

confidence: 99%

Characterization and Identification of a Chymotryptic Hydrolysate of Alpha-Lactalbumin Stimulating Cholecystokinin Release in STC-1 Cells

Catiau

Delval-Dubois

Guillochon

et al. 2011

Appl Biochem Biotechnol

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Alpha-lactalbumin hydrolysate is of significant interest, due to its potential application as a source of bioactive peptides in nutraceutical and pharmaceutical domains. This study was focused on the cholecystokinin (CCK) family compounds which are small peptides involved in the satiety control. The action of chymotryptic hydrolysate of alpha-lactalbumin on cholecystokinin release from intestinal endocrine STC-1 cells was investigated. We demonstrated for the first time that a chymotryptic hydrolysate of alpha-lactalbumin was able to highly stimulate CCK-releasing activity from STC-1 cells. The peptidic hydrolysate was characterized by LC/MS and MS/MS, thus highlighting the presence of 11 fractions containing 21 peptides, each potentially having the desired activity.

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Kinetic study of the appearance of an anti‐bacterial peptide in the course of bovine haemoglobin peptic hydrolysis

Cited by 34 publications

References 28 publications

Extraction of Proteins from Mackerel Fish Processing Waste Using Alcalase Enzyme

Extraction of Proteins from Mackerel Fish Processing Waste Using Alcalase Enzyme

Valorization of cruor slaughterhouse by-product by enzymatic hydrolysis for the production of antibacterial peptides: focus on α 1–32 family peptides mechanism and kinetics modeling

Characterization and Identification of a Chymotryptic Hydrolysate of Alpha-Lactalbumin Stimulating Cholecystokinin Release in STC-1 Cells

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