Ensieh Salehghamari, Mohammad Ali Amoozegar,
Volume 3, Issue 4 (3-2017)
Abstract
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< 0.05) was 120.4 U/mg.
Samaneh Khosroshahi, Ensieh Salehghamari, Mohammad Ali Amoozegar, Parvaneh Saffarian,
Volume 6, Issue 4 (1-2020)
Abstract
Nowadays plant endophytic bacteria have found diverse and useful applications in biotechnology; therefore, much attention has been paid to the isolation, identification, and evaluation of these microorganisms. Since the sterilizing plant tissue surfaces from epiphytic bacteria is difficulty, the efficacy of three different screening methods for endophytic bacteria including 1- HClO sterilization, 2- Periodic sterilization (modified tyndallization) and 3- Triton X100 and HClO sterilization, was evaluated in this study. The modified Tyndallization is an innovative method used in this study to appropriately remove the internal spores of epiphytic bacteria, considered to be an obstacle to the isolation of endophytes. Most of the endophytic bacteria were isolated from dicotyledons and leaves. Endophytic bacteria were also studied for the production of different hydrolase enzymes, whereas the protease enzyme was produced in a wide range of endophytic bacteria in greater quantities than other enzymes. The EndoA strain was molecularly identified and found to be 100% similar to Bacillus halotolerans.