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Etude De La Cinetique Dhydrolyse De La Caseine Beta Beta Bovine Par La Chymosine Et La Pepsine Bovines
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Book Synopsis Étude de la cinétique d'hydrolyse de la caséine [beta] [béta] bovine par la chymosine et la pepsine bovines by : Hervé Guillou
Download or read book Étude de la cinétique d'hydrolyse de la caséine [beta] [béta] bovine par la chymosine et la pepsine bovines written by Hervé Guillou and published by . This book was released on 1988 with total page 206 pages. Available in PDF, EPUB and Kindle. Book excerpt: L'étude de l'hydrolyse de la caséine [beta] bovine par la chymosine et la pepsine bovines a été réalisée in vitro.L'élévation du pH, aux alentours de 9, s'est révélé être un mode d'inhibition total, immédiat et quasiment irréversible des deux enzymes.Notre travail a commencé par la mise au point d'une méthode de dosage relatif des caséines, à partir de la caséine entière, par chromatographie liquide rapide d'échange d'ions. L'étude de différentes techniques d'analyse a montré que la méthode à l'acide trinitrobenzènesulfonique permet la détermination précise du degré de protéolyse. La chromatographie liquide haute performance sur colonne de phase inverse, en TFA/acétonitrile, a permis de séparer les peptides de la fraction soluble à pH 4,6 des hydrolysats. Leur identification a montré que certains peptides contiennent les fragments auxquels on attribue un rôle physiologique. Ces identifications ont permis de déterminer les liaisons hydrolysées et de comparer la spécificité d'hydrolyse des deux enzymes.L'étude de l'hydrolyse de la caséine [beta] sous l'effet du pH, a montré que le degré de protéolyse de la caséine [beta] par la chymosine est optimal à pH 4,5 et que le degré de protéolyse de la caséine [beta] par la pepsine augmente lorsque l'on se rapproche de pH 2. Cette étude a permis de déterminer le pH optimal de production de certains peptides chymosiques et pepsiques et montre que la pepsine est susceptible de libérer, dans l'intestin, un grand nombre de peptides dont ceux contenant les fragments auxquels on attribue un rôle physiologique. L'étude de 'hydrolyse de la caséine [beta], sous l'effet de la force ionique, a montré que le degré de protéolyse et que la production des peptides chymosiques et pepsiques diminuent lorsque la force ionique augmente.
Book Synopsis Comparaison de l'activité protéolytique de la chymosine et de la pepsine bovine sur la caséine entière et sur les caséines alpha(S1), apha(s2), bêta, kappa by : Yolanda Landeata de Ortiz
Download or read book Comparaison de l'activité protéolytique de la chymosine et de la pepsine bovine sur la caséine entière et sur les caséines alpha(S1), apha(s2), bêta, kappa written by Yolanda Landeata de Ortiz and published by . This book was released on 1977 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Effect of Genetic Variants on Hydrolysis of [beta]-casein by Chymosin and Pepsin by : Tharmalingam Jeyaragavan
Download or read book Effect of Genetic Variants on Hydrolysis of [beta]-casein by Chymosin and Pepsin written by Tharmalingam Jeyaragavan and published by . This book was released on 2001 with total page 194 pages. Available in PDF, EPUB and Kindle. Book excerpt: "Several studies have demonstrated that certain genetic variants of beta-casein are closely related to milk production, milk composition and technological properties of milk such as coagulation properties during cheese making, calcium precipitation and water binding properties. The objective of current study is to investigate the effect of the genetic variants on hydrolysis of beta-casein by chymosin and pepsin. On the basis of a preliminary analysis, a total of 50 milk samples which provided representatives of different available genetic variants of beta-casein were collected from different herds in Quebec. Casein was prepared from milk samples by the acid precipitation and the genetic variants of beta-casein were identified by both alkaline and acid urea-PAGE. An anion exchange chromatography was employed for the separation of beta-casein from whole casein. An initial hydrolysis of beta-casein of different phenotypes by chymosin and pepsin were achieved under the optimized hydrolytic conditions. Hydrolysates were periodically removed from the reaction mixture and they were analyzed by both RP-HPLC and SDS-PAGE in order to study the hydrolytic pattern of each beta-casein variant with the increasing hydrolytic time. (Abstract shortened by UMI.)" --
Book Synopsis Production of Bovine [beta]-casein in the Yeast Yarrowia Lipolytica by : Peter Douglas Roberts
Download or read book Production of Bovine [beta]-casein in the Yeast Yarrowia Lipolytica written by Peter Douglas Roberts and published by . This book was released on 1993 with total page 360 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Alternatives to Bentonite Fining by : Noel Millie Fong
Download or read book Alternatives to Bentonite Fining written by Noel Millie Fong and published by . This book was released on 1990 with total page 220 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Bovine [beta]-casein by : Anne Therese Flateau
Download or read book Bovine [beta]-casein written by Anne Therese Flateau and published by . This book was released on 1986 with total page 250 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Kinetic Study of the Association of Beta-casein by the Pressure-jump Method by : Ching-Hsia Cinnia Huang
Download or read book Kinetic Study of the Association of Beta-casein by the Pressure-jump Method written by Ching-Hsia Cinnia Huang and published by . This book was released on 1978 with total page 176 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis On the Specificity of Chymosin (rennin) in Its Action on Bovine B-casein by : S. Visser
Download or read book On the Specificity of Chymosin (rennin) in Its Action on Bovine B-casein written by S. Visser and published by . This book was released on 1977 with total page 15 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis UTILISATION DE LA TRYPSINE LIBRE ET IMMOBILISEE COMME SONDE D'ETUDE DE LA STRUCTURE DE LA MICELLE DE CASEINE BOVINE by : VALERIE.. GAGNAIRE
Download or read book UTILISATION DE LA TRYPSINE LIBRE ET IMMOBILISEE COMME SONDE D'ETUDE DE LA STRUCTURE DE LA MICELLE DE CASEINE BOVINE written by VALERIE.. GAGNAIRE and published by . This book was released on 1994 with total page 206 pages. Available in PDF, EPUB and Kindle. Book excerpt: BIEN QUE LE ROLE ET LA REPARTITION DE LA CASEINE KAPPA DANS LES MICELLES DE CASEINES BOVINES SOIENT CONNUS, CEUX DES CASEINES ALPHA S1 ET BETA RESTENT A ECLAIRCIR. NOS TRAVAUX ONT PORTE SUR L'ACCESSIBILITE DES CASEINES ALPHA S1 ET BETA DANS LA MICELLE EN UTILISANT COMME SONDE LA TRYPSINE, SOUS FORME LIBRE ET IMMOBILISEE SUR DES BILLES DE VERRE. IL APPARAIT QUE LA CASEINE BETA EST PLUS SENSIBLE A LA PROTEOLYSE QUE LA CASEINE ALPHA S1 DANS TOUTE LA STRUCTURE MICELLAIRE. NOUS AVONS AUSSI COMPARE LA SUSCEPTIBILITE A LA PROTEOLYSE DE CES CASEINES EN SOLUTION PURE. NOS RESULTATS ONT PERMIS D'OBTENIR DES INFORMATIONS SUR LEUR ETAT CONFORMATIONNEL DANS LES MICELLES. LA CASEINE BETA SERAIT SOUS FORME DE POLYMERE LACHE AVEC DES CHAINES POLYPEPTIDIQUES FLEXIBLES. L'INCORPORATION DE LA CASEINE ALPHA S1 S'ACCOMPAGNERAIT PAR CONTRE D'UNE REORGANISATION STRUCTURALE LORS DE SON ASSOCIATION AVEC LES AUTRES CASEINES ET SURTOUT AVEC LE PHOSPHATE DE CALCIUM COLLOIDAL. L'HYDROLYSE TRYPSIQUE, NOUS A PERMIS D'ISOLER ET D'IDENTIFIER LA MAJEURE PARTIE DES SEQUENCES PEPTIDIQUES PHOSPHORYLEES IMPLIQUEES DANS CES ASSOCIATIONS, A SAVOIR LES PHOSPHOPEPTIDES CONTENANT AU MOINS TROIS PHOSPHOSERINES, ISSUS EN TOTALITE DE LA CASEINE ALPHA S1 ET POUR MOITIE DE LA CASEINE BETA. NOS RESULTATS TENDENT A VALIDER UN MODELE DE STRUCTURE MICELLAIRE OUVERTE. LA CASEINE ALPHA S1 FORMERAIT UN MAILLAGE PAR ASSOCIATION AVEC LE PHOSPHATE DE CALCIUM COLLOIDAL, A L'INTERIEUR DUQUEL SERAIENT PRESENTES LES CASEINES KAPPA ET BETA. CETTE DERNIERE SERAIT PRESENTE SOUS FORME D'AGREGATS LACHES, DONT UNE MOITIE INTERAGIRAIT AVEC LE PHOSPHATE DE CALCIUM COLLOIDAL ET L'AUTRE SERAIT CAPABLE DE SE DEPLACER A L'INTERIEUR VOIRE DE SORTIR DE LA STRUCTURE MICELLAIRE.
Book Synopsis Kappa and Beta Casein by : Matthew J. Cherni
Download or read book Kappa and Beta Casein written by Matthew J. Cherni and published by . This book was released on 1979 with total page 124 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis A Genetic and Biochemical Analysis of [alpha][subscript S1]-casein and [beta]-casein in Bovine Species by : Jerry Caldwell
Download or read book A Genetic and Biochemical Analysis of [alpha][subscript S1]-casein and [beta]-casein in Bovine Species written by Jerry Caldwell and published by . This book was released on 1969 with total page 130 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Modification of Bovine Beta-casein Using Genetic Engineering and Its Structure/function Studies by : Byung-Kwon Choi
Download or read book Modification of Bovine Beta-casein Using Genetic Engineering and Its Structure/function Studies written by Byung-Kwon Choi and published by . This book was released on 1996 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: The putative glycosylation site (Asn-X-Ser) was introduced to the bovine $beta$-casein cDNA and genomic DNA (A$sp2$ genetic variant) using PCR-based site-directed mutagenesis to increase its amphiphilicity. The two mutant bovine $beta$-casein sequences containing the substitution of ${bf Ser}sb{70}$ for ${bf Leu}sb{70}$ (Asn$sb{68}$-Ser$sb{69}$-${bf Ser}sb{70}$-Pro$sb{71})$ and the substitution of ${bf Ser}sb{71}$ for ${bf Pro}sb{71}$ (Asn$sb68$-Ser$sb{69}$-${bf Ser}sb{70}$-${bf Ser}sb{71})$ were constructed and expressed using Pichia pastoris and transgenic mice. The mutant constructs were placed under the control of the methanol-inducible alcohol oxidase (AOX1) promoter for P. pastoris and of the bovine $alpha$-lactalbumin promoter for transgenic mice. The N-linked glycosylation of the mutant carrying Pro$sb{71}$ was completely inhibited whereas the other mutant carrying Ser$sb{71}$ was N-linked glycosylated in both expression systems. Thus, the C-terminal proline residue in the sequon was found to be a structural inhibitor for N-glycosylation. Glyco-$beta$-caseins produced in both systems were phosphorylated to the same degree as authentic bovine $beta$-casein. In addition, based on lectin blots, the oligosaccharides of glyco-$beta$-casein from P. pastoris were high-mannose type whereas transgenic glyco-$beta$-caseins contained various oligosaccharide chains. Mouse casein micelles containing glycosylated bovine $beta$-casein showed the largest median diameter and rough outer surfaces, compared to normal mouse casein micelles and micelles from transgenic milk containing wild-type bovine $beta$-casein.
Book Synopsis Effect of Genetic Variants on Hydrolysis of Bovine K-casein by Chymosin and Pepsin by : Julius J. Jefferson
Download or read book Effect of Genetic Variants on Hydrolysis of Bovine K-casein by Chymosin and Pepsin written by Julius J. Jefferson and published by . This book was released on 2002 with total page 196 pages. Available in PDF, EPUB and Kindle. Book excerpt: "Caseins are present in milk in the form of large spherical complexes called micelles that are stabilized by kappa-casein found on the surface. This stabilizing effect is lost when milk clotting enzymes hydrolyze kappa-casein thereby initiating the coagulation process. The objective of this study was to analyze the effect of kappa-casein polymorphism upon hydrolysis by proteases. The A and B forms are the most common genetic variants of kappa-casein in Canadian Holstein dairy herds, representing three phenotypes AA, AB and BB. Whole casein from Holstein milk samples was fractionated into its four major components by ion-exchange chromatography using Express Ion Exchanger Q Anion Exchanger and Macro-Prep High Q Anion Exchange Support columns. The kappa-casein fraction was isolated, dialyzed, and assessed for its phenotype and purity by PAGE. The pure forms of the three different phenotypes of kappa-casein (AA, AB, BB) at a final concentration of 0.5% were then hydrolyzed by calf chymosin (1:500) and porcine pepsin (1:1000) at a pH of 5.8 at 37°C. Aliquots were collected at 0, 5, 15, 30, 60 and 90 min and the reaction stopped by using 24% NH4OH. The rate of hydrolysis of the three phenotypes was analyzed by comparing the disappearance of the substrate with time from the RP-HPLC chromatograms using Waters MAXIMA software. SDS-PAGE was used to calculate the approximate molecular weight of the hydrolytic products. Analysis of the hydrolysate profiles indicated that there was significant difference (P
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