جستجوی مقالات مرتبط با کلیدواژه « فعالیت ویژه » در نشریات گروه « زیست شناسی »

Lepidium draba peroxidase (LDP) belonging to the class III plant peroxidases that its amino acid sequence shows over 90% similarity with horseradish peroxidase (HRP).

In this study, after expression and purification of LDP, its immobilization conditions were optimized on the Zinc metal-organic framework (Zn-MOF) using glutaraldehyde as a cross-linking agent for firm binding. Then physicochemical properties, kinetic parameters and stability of the immobilized enzyme were compared with the free one.

The best conditions for enzyme immobilization with 67% yield were optimized at concentration of 0.02 g of Zn-MOF, 0.75mg/ml and 1.2 dM of glutaraldehyde, after 3h incubation. The results showed that the specific activity of the immobilized enzyme increased more than doubled that of free enzyme and its Km was reduced by 49% compared to the free one for TMB substrate. Also its kinetic stability reduced against pH and temperature in compared to the free enzyme.

Lipase is one of the most important hydrolytic enzymes widely used in various commercial activities such as food, dairy, pharmaceutical and detergent inducteries. In this experiment, Taguchi method was attempted as a powerful method to optimize the factors affecting enzyme production and to investigate the interactions among these factors and their optimum combination in Salinivibrio sp. SA2. The optimum conditions for pH, temperature, shaker's rpm, olive oil concentration and salt type turned out to be 8, 35 °C, 100 rpm, 2% and sodium chloride 1 M, respectively. Significant factors influencing on the lipase production proved to be pH, agitation and Salt type. The maximum lipase activity in optimum condition and at the 5% significance level (p