IMMOBILIZATION OF ALPHA-AMYLASE INTO GELATIN FILMS WITH VARIOUS CROSS-LINKERS

1992-05-01
BAYRAMOGLU, Z
Akbulut, Ural
SUNGUR, S
Show full item record
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
174
views
0
downloads
This article reports the cross linking of alpha-amylase enzyme to gelatin by using formaldehyde, chromium (III) acetate, chromium (III) sulfate and potassium chromium (III) sulfate as hardeners. The effect of concentrations of cross linkers, enzyme and gelatin on the activity of immobilized enzyme were investigated.
https://hdl.handle.net/11511/35641
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Department of Chemistry, Article

Suggestions

IMMOBILIZATION OF ALPHA-AMYLASE INTO PHOTOGRAPHIC GELATIN BY CHEMICAL CROSS-LINKING
BAYRAMOGLU, Z; Akbulut, Ural; SUNGUR, S (Elsevier BV, 1992-01-01)
Alpha-amylase was immobilized into photographic gelatin by chemical cross-linking with chromium (III) acetate and chromium (III) sulphate. Cellulose triacetate film strips, enabled simple handling when coated with an alpha-amylase-gelatin mixture, accomplishing a high degree of durability during consecutive immersions into reaction media. The optimum conditions for pH, substrate concentration, temperature, incubation time and storing conditions of free and immobilized alpha-amylase were determined. The effe...
Compatibilization of poly(2,6-dimethyl-1,4-phenylene oxide) and poly(2,6-dichloro-1,4-phenylene oxide) with sulfonated polystyrene and its Na and Zn-neutralized ionomers
Mih, M; Aras, L; Alkan, C (Springer Science and Business Media LLC, 2003-05-01)
Compatibility of acidic (H), Na, and Zn neutralized sulfonated polystyrene ionomer blends with Poly(2,6-dimethyl-1,4-phenylene oxide) (PPO) and Poly(2,6-dichloro-1,4-phenylene oxide) (PDCIPO) was investigated by Dilute Solution Viscometry (DSV) and Differential Scanning Calorimetry (DSC). The intrinsic viscosities of the blends, are measured in suitable solvents. The degree of compatibility of the blends is characterized by Ab parameter. According to the results, PPO is completely miscible, except for Na-ne...
STUDIES ON IMMOBILIZATION OF UREASE IN GELATIN BY CROSS-LINKING
SUNGUR, S; ELCIN, YM; Akbulut, Ural (Elsevier BV, 1992-01-01)
Urease enzyme was immobilized in photographic gelatin by chemical cross-linking using formaldehyde, glutaraldehyde and chromium (III) acetate. The effects of enzyme and cross-linker concentrations, temperature, incubation time and pH on urea hydrolysis were investigated. Effect of reuse on the activity of immobilized enzyme was also studied. Glutaraldehyde (0.004 M) was the most suitable cross-linker; relative activities within 2.5 months after 24 reuses were stable (about 78%).
Immobilization of dioxomolybdenum(VI) complex bearing salicylidene 2-picoloyl hydrazone on chloropropyl functionalized SBA-15: A highly active, selective and reusable catalyst in olefin epoxidation
Bagherzadeh, Mojtaba; Zare, Maryam; Salemnoush, Taghi; Özkar, Saim; Akbayrak, Serdar (Elsevier BV, 2014-04-05)
A novel organic-inorganic hybrid heterogeneous catalyst system was obtained from the reaction of the molybdenum(VI) complex of salicylidene 2-picoloyl hydrazone with mesoporous silica containing 3-chloropropyl groups prepared by a direct synthetic approach involving hydrolysis and co-condensation of tetraethylorthosilicate (TEOS) and 3-chloropropyltrimethoxysilane in the presence of the triblock copolymer P123 as template under acidic conditions. Characterization of the functionalized materials by X-ray dif...
Immobilization of glucose isomerase in surface-modified alginate gel beads
TÜMTÜRK, HAYRETTİN; DEMİREL, Gökhan; ALTINOK, HAYDAR; AKSOY, SERPİL; Hasırcı, Nesrin (2008-04-01)
In this study, glucose isomerase enzyme was entrapped into modified and nonmodified calcium alginate gel beads. Various characteristics of free and immobilized enzymes such as the optimum pH, temperature and dependence of activity on storage and operational stability were evaluated. The optimum pH and temperature of free and immobilized glucose isomerase were found to be the same values as 7.5 and 60C, respectively. For free and immobilized enzymes, kinetic parameters were calculated as 1.79 x 10(-2) and 8....
Citation Formats
Z. BAYRAMOGLU, U. Akbulut, and S. SUNGUR, “IMMOBILIZATION OF ALPHA-AMYLASE INTO GELATIN FILMS WITH VARIOUS CROSS-LINKERS,” BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, pp. 427–432, 1992, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/35641.
METU IIS - Integrated Information Service open@metu.edu.tr