A Highly Thermostable Xylanase from Stenotrophomonas maltophilia: Purification and Partial Characterization
نویسندگان
چکیده
Seven xylanolytic bacterial strains were isolated from saw-dust dump soil. The bacterial strain X6 was selected on the basis of the highest xylanase activity with no cellulase contamination. It was identified as Stenotrophomonas maltophilia by biochemical tests and 16S rRNA gene sequencing approach. Xylanase production studies by S. maltophilia on different commercial xylans and agro-industrial residues suggested that wheat bran was the best carbon source for xylanase production (26.4 ± 0.6 IU/mL). The studies with inorganic and organic nitrogen sources suggested yeast extract as the best support for xylanase production (25 ± 0.6 IU/mL). Maximum xylanase production was observed at initial medium pH = 8.0 (23.8 ± 0.4 IU/mL) with production at pH = 7.0 and pH = 9.0 being almost comparable. Xylanase produced by S. maltophilia was purified to homogeneity using ammonium sulfate precipitation, gel filtration, and ion exchange chromatography. The final purification was 5.43-fold with recovery of 19.18%. The molecular weight of the purified xylanase protein was ~142 kDa. Both crude and purified xylanase had good stability at pH = 9.0 and 80°C with activity retention greater than 90% after 30 min incubation. The enzyme stability at high temperature and alkaline pH make it potentially effective for industrial applications.
منابع مشابه
Whole-Genome Sequence of Stenotrophomonas maltophilia ZBG7B Reveals Its Biotechnological Potential
Stenotrophomonas maltophilia ZBG7B was isolated from vineyard soil of Zellenberg, France. Here, we present the draft genome sequence of this bacterial strain, which has facilitated the prediction of function for several genes encoding biotechnologically important enzymes, such as xylosidase, xylanase, laccase, and chitinase.
متن کاملPurification, characterization, gene cloning and expression of GH-10 xylanase (Penicillium citrinum isolate HZN13)
An extracellular thermostable xylanase (Xyl-IIb) produced by Penicillium citrinum isolate HZN13 was purified to homogeneity using DEAE-Sepharose, Sephadex G-100 and Bio-Gel P-60 chromatography with specific activity of 6272.7 U/mg and 19.6-fold purification. The purification revealed the occurrence of multiple forms of xylanases (Xyl-I, Xyl-IIa, Xyl-IIb and Xyl-III). The molecular mass of highl...
متن کاملProduction, Partial Purification and Biochemical Characterization of Thermostable Xylanase from Bacillus brevis
Additional to industrial use of xylanase in kraft pulp production, thermostable xylanase has wider application in fishery, piggery, cattle food and human food. In this research, 1-4-β-Dendoxylanase was isolated from liquid state cultures of Bacillus brevis containing wheat straw as carbon source. Xylanase was purified to apparent homogeneity by gel filtration and ion exchange chromatography. Th...
متن کاملCharacterization of small-colony-variant Stenotrophomonas maltophilia isolated from the sputum specimens of five patients with cystic fibrosis.
Cystic fibrosis (CF) patients are predisposed to chronic respiratory infection by nonfermentative gram-negative bacilli, including Stenotrophomonas maltophilia. S. maltophilia is highly resistant to most antibiotics, with the exception of sulfamethoxazole-trimethoprim (SXT). SXT-resistant S. maltophilia has been reported, but the mechanism of resistance is not well defined. Repeated findings of...
متن کاملPurification and Characterization of a Novel Thermostable and Acid Stable α-Amylase from Bacillus Sp. Iranian S1
This study reports the purification and biochemical characterization of thermostable and acidic-pH-stable α-amylase from Bacillus sp. Iranian S1 isolated from the desert soil (Gandom-e-Beryan in Lut desert, Iran). Amylase production was found to be growth associated. Maximum enzyme production was in exponential phase with activity 2.93 U ml-1 at 50°C and pH 5. The enzyme was purified by isoprop...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
دوره 2013 شماره
صفحات -
تاریخ انتشار 2013