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overcome these problems, cellulase immobilization is established. The process of immobilization eliminates enzyme recovery and purification. Further, it aids in the enzyme utilization and better environment for biocatalytic reactions. The technique also

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homogeneous catalysts. Mixed metal exchanged zeolite, ion exchanged resins [ 20 ] and polymerized complexes [ 21 ] have been used in the liquid phase epoxidation of olefins [ 22 ]. Recent trends in the immobilization of catalyst complexes on clay

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different heterojunction system and utilizing thin film. Furthermore, immobilization of TiO 2 powder on solid supports is an alternative convenient method to solve the post-treatment catalyst recovering problem. The photocatalytic efficiency of the

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dichloromethane for 72 h. In this stage, NaY–FeTMePP porphyrin placed within cages of zeolite. The solid had pale brown color. Immobilization of TMePP inside the MnNaY and CoNaY carried out by the same method as FeNaY. Catalyst

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Ruminant Res. , 68 , 64 – 72 . Ganapathy , R. , Manolache , S. , Sarmadi , M. & Denes , F. 2001 : Immobilization of papain on cold

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Acta Microbiologica et Immunologica Hungarica
Authors: S. S. Kanwar, M. Srivastava, S. S. Chimni, I. A. Ghazi, R. K. Kaushal, and G. K. Joshi

Brady, C., Metacalfe, L., Slaboszewski, D., Frank, D.: Lipase immobilized on a hydrophobic, microporous support for the hydrolysis of fats. J Am Oil Chem Soc 65 , 917-921 (1988). Lipase

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Abstract  

The unfolding of α-chymotrypsinogen covalently immobilized on silica beads has been studied by differential scanning calorimetry (DSC). The enzyme undergoes an unfolding transition which, unlike the free protein, cannot be approximated by a single two-state process. After immobilization, the unfolding is characterized by the presence of two partially overlapping transitions, both of them show two-state behavior. The two processes correspond to the separate unfolding of the two domains of the α-chymotrypsinogen molecule. The loss of cooperativity behavior is a consequence of the covalent immobilization. The two domains showed different thermal stability as functions of pH. One of them unfolded with a transition temperature T m2 higher than T m of the free enzyme, implying stabilization effect of immobilization. However, below pH 4.5, its native structure is lost. The other transition shows a remarkable pH-independent thermal stability from pH 2.5 to 7.0.

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Kreeger, T. J., Arnemo, J. M. and Raath, J. P. (2002): Handbook of Wildlife Chemical Immobilization: International Edition. Wildlife Pharmaceuticals, White River, Mpumalanga, South Africa. Raath J. P

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Gueguen, Y., Chemardin, P., Pien, S., Arnaud, A. & Glazy, P. (1997): Enhancement of aromatic quality of Muscat wine by the use of immobilized β-glucosidase. J. Biotechnol. , 55 , 151

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Introduction Glasses and glass–ceramic materials currently find applications in various fields of science and technology. As of now, the current task is the utilization of glasses and glass–ceramics for the immobilization of

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