9786139899234 - Expression, Purification and Characterization of recombinant Xylanases di Patel, Hetal; Panchal, Malti; Patel, Niyati (10 risultati)

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Taschenbuch. Condizione: Neu. Expression, Purification and Characterization of recombinant Xylanases | Hetal Patel (u. a.) | Taschenbuch | 84 S. | Englisch | 2018 | LAP LAMBERT Academic Publishing | EAN 9786139899234 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.

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Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -The book aims to compare some of the kinetic properties of covalently immobilized xylanase on the surface of glutaraldehyde activated alginate beads with free xylanase. Immobilization is defined as the imprisonment of cell or enzyme in a distinct support or matrix. The support or matrix on which the enzymes are immobilized allows the exchange of medium containing substrate or effector or inhibitor molecules. The practice of immobilization of cells is very old and the first immobilized enzyme was amino acylase of Aspergillus oryzae for the production of L-amino acids in Japan. The immobilized enzyme displayed higher Vmax, Km and kcat values but lower kcat/Km value in comparison to its free counterpart. Overall, the 'catalytic efficiency' of xylanase was found to decline with immobilization. The isokinetic temperature (Tisokin) of free and immobilized xylanase was recorded at 86.5ºC with ln kd value of about -4.0. The method of immobilization provided 'low temperature stabilization' effect to xylanase which makes it more thermostable at temperatures lower than the Tisokin. 84 pp. Englisch.

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Condizione: New. PRINT ON DEMAND.

Condizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Patel HetalHetal Patel, completed her Master s at Charusat University, Changa, Anand, India in 2012. She is currently working as Research associate at Cliantha CRO, Ahmedabad.The book aims to compare some of the kinetic propertie.

Taschenbuch. Condizione: Neu. This item is printed on demand - Print on Demand Titel. Neuware -The book aims to compare some of the kinetic properties of covalently immobilized xylanase on the surface of glutaraldehyde activated alginate beads with free xylanase. Immobilization is defined as the imprisonment of cell or enzyme in a distinct support or matrix. The support or matrix on which the enzymes are immobilized allows the exchange of medium containing substrate or effector or inhibitor molecules. The practice of immobilization of cells is very old and the first immobilized enzyme was amino acylase of Aspergillus oryzae for the production of L-amino acids in Japan. The immobilized enzyme displayed higher Vmax, Km and kcat values but lower kcat/Km value in comparison to its free counterpart. Overall, the 'catalytic efficiency' of xylanase was found to decline with immobilization. The isokinetic temperature (Tisokin) of free and immobilized xylanase was recorded at 86.5ºC with ln kd value of about -4.0. The method of immobilization provided 'low temperature stabilization' effect to xylanase which makes it more thermostable at temperatures lower than the Tisokin.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 84 pp. Englisch.

Taschenbuch. Condizione: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - The book aims to compare some of the kinetic properties of covalently immobilized xylanase on the surface of glutaraldehyde activated alginate beads with free xylanase. Immobilization is defined as the imprisonment of cell or enzyme in a distinct support or matrix. The support or matrix on which the enzymes are immobilized allows the exchange of medium containing substrate or effector or inhibitor molecules. The practice of immobilization of cells is very old and the first immobilized enzyme was amino acylase of Aspergillus oryzae for the production of L-amino acids in Japan. The immobilized enzyme displayed higher Vmax, Km and kcat values but lower kcat/Km value in comparison to its free counterpart. Overall, the 'catalytic efficiency' of xylanase was found to decline with immobilization. The isokinetic temperature (Tisokin) of free and immobilized xylanase was recorded at 86.5ºC with ln kd value of about -4.0. The method of immobilization provided 'low temperature stabilization' effect to xylanase which makes it more thermostable at temperatures lower than the Tisokin.