Some Properties of a New Thermostable Xylanase from Alkaliphilic and Thermophilic Bacillus sp Isolate DM-15


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Ozcan B. D. , Çoşkun A., Özcan N. , Baylan M.

JOURNAL OF ANIMAL AND VETERINARY ADVANCES, vol.10, no.2, pp.138-143, 2011 (Journal Indexed in SCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 10 Issue: 2
  • Publication Date: 2011
  • Doi Number: 10.3923/javaa.2011.138.143
  • Title of Journal : JOURNAL OF ANIMAL AND VETERINARY ADVANCES
  • Page Numbers: pp.138-143
  • Keywords: Thermostable xylanase, Bacillus sp., characterization, optimum, molecular weight, thermal spring, ALPHA-AMYLASE, MICROBIAL XYLANASES, ALKALINE XYLANASES, PURIFICATION, CELLULASE, ENZYMES, GENE, MICROORGANISMS, CLONING

Abstract

Alkaliphilic and thermophilic Bacillus sp. DM-15 was isolated from ciftehan thermal spring, Turkey, produced thermostable xylanase at 55 degrees C at pH 9. The molecular weight of the enzyme was estimated to be 95.6 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The enzyme showed broad working pH range of 4.5-10.0 with art optimum pH of 6.5. The temperature optimum of the enzyme was found to be 60-70 degrees C. Xylanase production by thermophilic Bacillus sp. strain cultivated in liquid media reached a maximum at 36h, with levels of 192.8 mu mol mg(-1) protein/min. The enzyme was stable for 15 min at 60 degrees C while 13, 86, 95 and 96% of the original activities were lost at 70, 80, 90 and 100 C, respectively. Enzyme activity was increased in the presence of 5 mkt CaCl2 (137%), CoCl2 (133%), CuSO4 (112%), MgCl2 (106%) and KCl (105%) and inhibited in the presence of 5 mMEDTA, HgCl2, FeSO4, SDS (1%), MnCl2, Triton X-100 (1%) up to 93, 89, 73, 41,29 and 8%, respectively. The DM-15 thermostable xylanase may be suitable for several industrial applications, such as food, agricultural and biofuel.