STABILITY AND STORAGE-CONDITIONS OF NADH-CYTOCHROME B5 REDUCTASE CROSS-LINKED INTO GELATIN BY CHROMIUM(III) ACETATE

1994-06-01
NADH-cytochrome b5 reductase was isolated and partially purified from rabbit liver microsomes. It was immobilized into gelatin by chemical cross-linking. Chromium (III) acetate was used as cross-linker. The effects of pH and temperature on the immobilized cytochrome b5 reductase were investigated. The reusability and storage stability of immobilized enzyme were also tested. Immobilized NADH-cytochrome b5 reductase activities were found to be stable for at least 72 d and 24 uses. The storage stability of NADH-cytochrome b5 reductase was improved with immobilization at 25 degrees C.

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...
Characterization of sheep liver N-acetyltransferase
Güray, Nülüfer Tülün (1997-05-01)
Acetyl-coenzyme A (AcCoA)-dependent arylamine N-acetyltransferase (NAT:EC 2.3.1.5) was isolated from sheep liver and the specific activity was found as 5.3+/-1.4x10(-3) (mean+/-SE, n=8) nmoles/ min/ mg protein. The effects of p-aminobenzoic acid (PABA) and acetylCoA concentrations, pH, amount of enzyme and reaction period, on the enzyme activity were also studied and the optimum conditions for maximum activity of sheep liver NAT was determined. Sulfamethazine (SMZ) was used as a substrate in order to study ...
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 glucose oxidase in poly(2-hydroxyethyl methacrylate) membranes
Arica, Y.; Hasirci, V.N.; Arica, Yakup (Elsevier BV, 1987-11)
Glucose oxidase (GOD) was immobilized in a poly(2-hydroxyethyl methacrylate) (HEMA) membrane through matrix entrapment in order to investigate the effect of various parameters (e.g. concentration of ingredients, temperature, repeated interaction with glucose and shelf storage) on the activity of the enzyme. Permeability of the membrane to a model permeant was tested and SEMs were obtained. It was observed that upon immobilization the affinity of GOD towards glucose was substantially decreased, and increasin...
POLYESTER FILM STRIPS COATED WITH PHOTOGRAPHIC GELATIN CONTAINING IMMOBILIZED GLUCOSE-OXIDASE HARDENED BY CHROMIUM(III) SULFATE
ELCIN, YM; Akbulut, Ural (Elsevier BV, 1992-01-01)
Glucose oxidase was immobilized into photographic gelatin hardened by chromium(III) sulphate. The enzyme-gelatin mixture was coated on polyester film strips which allowed easy and simple handling during assays. The effect of gelatin and cross-linker concentrations on water content and enzymatic activity was studied. The effect of pH during immobilization and that of incubation temperature on maximum activity were examined- Enzyme leakage tests were carried out during reuse number studies. Consecutive use of...
Citation Formats
O. Yıldırım and U. Akbulut, “STABILITY AND STORAGE-CONDITIONS OF NADH-CYTOCHROME B5 REDUCTASE CROSS-LINKED INTO GELATIN BY CHROMIUM(III) ACETATE,” BIOMATERIALS, pp. 587–592, 1994, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/36660.