Affiliation:
1. AVRASYA ÜNİVERSİTESİ
2. KARADENİZ TEKNİK ÜNİVERSİTESİ
Abstract
In this study, esterase of Aneurinibacillus sp. PDF24 strain, a thermophilic bacteria, was purified to homogenity (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 40 ºC, 50 ºC and 60 ºC for 1 hour. Km and Vmax values for p-nitrophenyl butyrate were determined as 0.120 mM and 3164.8 U/mg, respectively. 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.
Publisher
Sakarya University Journal of Science
Reference25 articles.
1. [1] S. Benjamin, and A. Pandey, “Candida rugosa Lipases: Molecular Biology and Versatility In Biotechnology.,” Yeast, vol. 14, pp. 1069–1087, 1998.
2. [2] R.D. Schmid, and R. Verger, “Lipases: Interfacial Enzymes with Attractive Applications,” Angewandte Chemie-International Edition, vol. 37, pp. 1608-1633, 1998.
3. [3] A. Svendsen, P. Woolley, and S. B. Petersen, “Lipases—Their Structure, Biochemistry and Applications.” Cambridge University Press, Cambridge, pp. 1–21, 1994.
4. [4] U. T. Bornscheuer, and R. J. Kazlauskas, “Hydrolayses In Organic Synthesis Regio and Stereoselective Biotransformations,” Wiley Vch, Weinheim, pp. 105 , 1999.
5. [5] P. K. Ghosh, R. K. Saxena, R. Gupta, R. P. Yadav, and S. Davidson, “Microbial Lipases Production and Applications” Science Progress, vol. 79, no. 2, pp. 119-157, 1996.