Characterization of a New Thermostable Carboxylesterase from Aneurinibacillus sp. PDF24

Authors : Meral BELDUZ KOLCU, Fulya AY SAL, Ali BELDÜZ, Sabriye ÇANAKÇI

Pages : 956-966

Doi:10.16984/saufenbilder.1074637

View : 34 | Download : 10

Publication Date : 2022-10-20

Article Type : Research Paper

Abstract :In this study, esterase of Aneurinibacillus sp. PDF24 strain, a thermophilic bacteria, was purified to homogenity insert ignore into journalissuearticles values(5.25 fold purification); by column chromotography, and characterized. The molecular weight of Aneurinibacillus sp. PDF24 esterase was determined about 40 kDa. The maximum activity of the purified esterase was analyzed at 55°C, pH 8.5. The esterase was found to be stable at 40ºC, 50ºC and 60ºC for 1 hour. Km and Vmax values for p-nitrophenyl butyrate were determined as 0.120 mM and 3164.8 U/mg, respectively. Considering Km values in the literature, Aneurinibacillus sp. PDF24 esterase was found to have a good Km value compared to other esterases. In the presence of 1 mM and 5 mM metal salts of Mg2+, Li+, Ca2+, K+, no significant change occured in enzyme activity. The activity of Aneurinibacillus sp PDF24 esterase was found to be stable also in the presence of ethanol, DMSO, EDTA, DTT and ß-mercaptoethanol. The data obtained suggest that the enzyme is a serine esterase, not a metalloprotein, and that disulfide bonds are not required to maintain enzyme conformation, and therefore, depending on its features, this esterase may be a suitable candidate for industrial applications.
Keywords : Aneurinibacillus, characterization, esterase, thermophilic