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    Purification and characterization of an alkaline pectin lyase produced by a newly isolated brevibacillus borstelensis (p35) and its applications in fruit juice and oil extraction
    (Springer Verlag, 2014) Demir N.; Nadaroglu H.; Demir Y.; Isik C.; Taskin E.; Adiguzel A.; Gulluce M.
    An alkaline pectin lyase (Pnl) (EC 4.2.2.10) secreted by Brevibacillus borstelensis P35 (genBank number: FJ417406) was purifed using ammonium sulfate fractionation, anion exchange chromatography on DEaE-cellulose and gel fltration chromatography on Sephadex g-150. The pH and temperature optima of the enzyme were found to be 8.0 and 60 °C. The enzyme does not loose activity up to 60 °C if exposed for 1 h. The values of Kmand Vmax of the enzyme were 0.625 mg/ml and 126.32 s-1, respectively. The molecular weight was found to be 36 ± 01 kDa. The presence of 10 mM concentration of Ca2+, Cu2+, Mn2+, Mg2+, Zn2+, Hg2+, Fe2+ and EDTa, L-cystein, ascorbic acid signifcantly enhanced the Pnl of the purifed enzyme. In the course of the laboratory trials, it was demonstrated that Pnl from B. borstelensis (P35) could be successfully applied to the production and clarif-cation of fruit juice and oil extraction. © Springer-Verlag Berlin Heidelberg 2014