Dergiler / Turkish Journal of Biology / 2009 / Cilt: 33 - Sayı: 3

Production and characterization of multifunctional endoxylanase by Bacillus sp. X13

Sayfa
231–237
Yayın Tarihi
2009-03-01
DOI
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The properties of the enzyme presented in this study suggest that this enzyme could be a potential industrial interest.

📌 3 Maddede Bu Makale

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Amaç & Hipotez:A multifunctional endoxylanase producing Bacillus sp. was isolated from soil.
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Temel Bulgular & Veri:Enzyme synthesis occurred at temperatures between 20 °C and 60 °C with an optimum 37 °C.
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Sonuç & Katkı:The properties of the enzyme presented in this study suggest that this enzyme could be a potential industrial interest.
🔬Tür:Araştırma Makalesi
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Key words: Bacillus sp. · extracellular · endoxylanase

Özet

A multifunctional endoxylanase producing Bacillus sp. was isolated from soil. Enzyme synthesis occurred at temperatures between 20 °C and 60 °C with an optimum 37 °C. Analysis of the enzyme by SDS-PAGE revealed 4 active enzyme bands, which were estimated to be 66.5 kDa, 80.6 kDa, 95.5 kDa, and 108.4 kDa. The enzyme has a broad temperature range, between 20 and 90 °C, with an optimum at 40 °C; and maximum activity was at pH 6.0. The enzyme showed a gradual decrease in the remaining activity as the pre-incubation temperature increase. Thermostability was not also increased in the presence of Ca2+. An average of 71% of remaining activity observed when the enzyme incubated between pH 3.6 and 10 for 1 h. The enzyme was highly inhibited by urea, and fairly inhibited by Triton X-100, CaCl2, ZnCl2, KCl, Na2SO3 PMSF, and 2-Mercaptoethanol. The properties of the enzyme presented in this study suggest that this enzyme could be a potential industrial interest.

Abstract

A multifunctional endoxylanase producing Bacillus sp. was isolated from soil. Enzyme synthesis occurred at temperatures between 20 °C and 60 °C with an optimum 37 °C. Analysis of the enzyme by SDS-PAGE revealed 4 active enzyme bands, which were estimated to be 66.5 kDa, 80.6 kDa, 95.5 kDa, and 108.4 kDa. The enzyme has a broad temperature range, between 20 and 90 °C, with an optimum at 40 °C; and maximum activity was at pH 6.0. The enzyme showed a gradual decrease in the remaining activity as the pre-incubation temperature increase. Thermostability was not also increased in the presence of Ca2+. An average of 71% of remaining activity observed when the enzyme incubated between pH 3.6 and 10 for 1 h. The enzyme was highly inhibited by urea, and fairly inhibited by Triton X-100, CaCl2, ZnCl2, KCl, Na2SO3 PMSF, and 2-Mercaptoethanol. The properties of the enzyme presented in this study suggest that this enzyme could be a potential industrial interest.

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Bu Makaleye Atıf Yap

AYGAN, A., ARIKAN, B. (2009). Production and characterization of multifunctional endoxylanase by Bacillus sp. X13. Turkish Journal of Biology, Cilt: 33 - Sayı: 3, 231–237. https://ajindex.com/articles/182171

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Kaynakça (14)

  1. Subramaniyan S, Prema P. Biotechnology of microbial Xylanases: enzymology, molecular biology and application. Crit Rev Biotechnol 22 (1): 33-46,2002. Gessesse A. Purification and properties of two thermostable alkaline xylanases from an alkaliphilic Bacillus sp. Appl Environ Microbiol 64: 3533- 3535, 1998.
  2. Voget S, Steele HL, Streit WR. Characterization of metagenome- derived halotolerant cellulase. J Biotechnol 126: 26- 36, 2006.
  3. Bernhardsdotter ECMJ, Ng JD, Garriott OK et al. Enzymic properties of an alkaline chelator-resistant a-amylase from alkaliphilic Bacillus sp. isolate L1711. Process Biochem 40: 2401- 2408, 2005.
  4. Burhan A, Nisa U, Gokhan C et al. Enzymatic properties of a novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT- 6. Process Biochem 38: 1397- 1403, 2003.
  5. Lo HF, Lin LL, Chen HL et al. Enzymatic properties of a SDS- resistant Bacillus sp. TS- 23 a-amylase produced by recombinant Escherichia coli. Process Biochem 36: 743- 750, 2001. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277: 680- 685, 1970.
  6. Bollag DM, Rozycki MD, Edelstein SJ. Protein methods. Willey- Liss Inc. New York; 1996.
  7. Maniatis T, Fritsch EF, Sambrook J. Molecular cloning: a laboratory manuel. Cold Spring Harbor Laboratory Pres. New York; 1982.
  8. Saul DJ, Williams LC, Grayling RA et al. ceIB, a Gene coding for a bifunctional cellulase from the extreme thermophile “Caldocellum saccharolyticum“. Appl Environ Microbiol 56: 3117- 3124, 1990.
  9. Singh J, Batra N, Sobti RC. Purification and characterization of alkaline cellulase produced by a novel isolate, Bacillus sphaericus JS1. J Ind Microbiol Biotechnol 31: 51- 56, 2004.
  10. Lopez C, Blanco A, Pastor FIJ. Xylanase production by a new alkali tolerant Bacillus. Biotechnol Lett 20: 243- 246, 1998.
  11. Tseng MJ, Yap MN, Ratanakhanokchai K et al. Purification and characterization of two cellulase free xylanase from an alkaliphilic Bacillus firmus. Enzyme Mibrob Technol 30: 590- 595, 2002.
  12. Ryan SE, Nolan K, Thompson R et al. Purification and characterization of a new low molecular weight endoxylanase from Penicillium capsulatum. Enzyme Microb Tehcnol 33: 775- 785, 2003.
  13. Gallordo O, Diaz P, Pastor FIJ. Cloning and characterization of xylanase A from the strain Bacillus sp. BP- 7: Comparison with alkaline pI-low molecular weight xylanase of family 11. Curr Microbiol 48: 276- 279, 2004.
  14. Collins T, Gerday C, Feller G. Xylana