Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates

Yıl: 2006 Cilt: 30 Sayı: 1 Sayfa Aralığı: 45 - 50 Metin Dili: Türkçe İndeks Tarihi: 29-07-2022

Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates

Öz:
Bu çalışmada üreme ve selüloz kullanım kapasiteleri bakımından bazı farklılıklar gösteren 13 ayrı termofilik, selülolitik, anaerobik, etanol üreticisi bakteri izolatının selülozomlarının CBM kodlayan bölgeleri PCR ile çoğaltılmış ve DNA dizileri saptanmıştır. Amplikonların kıyaslanan bölgelerinin DNA dizi analizleri, katı besiyerinde en yüksek selüloz kullanım kapasitesine sahip 7-9-1 suşunu da içeren 7 izolata ait CBM nükleotid ve amino asit dizilerinin Clostridium thermocellum'a ait CipB ile % 100 benzerliğe sahip olduklarını ortaya çıkarmıştır. Diğer yandan, yine yüksek selüloz kullanım kapasitesine sahip bir izolat olan 7-1-2 'ye ait CBM, 100 amino asitten 66'sında (%66) farklılık göstermiştir. Düşük selüloz kullanım kapasitesine sahip bir izolat olan 7-9-4 suşunda ise 118 amino asitten yalnızca 4'ünün farklı olduğu görülmüştür.
Anahtar Kelime: termofilik bakteriler yıkılma DNA dizi analizi karbonhidratlar selüloz seluloz sindirimi bağlanma bölgeleri Clostridium thermocellum selülolitik mikroorganizmalar polimeraz zincir reaksiyonu

Konular: Biyoloji

Çeşitli selülolitik, termofilik, anaerobik, etanol üreticisi izolatlarda karbonhidrat bağlanma modüllerinin birincil yapıları

Öz:
In the present study, the carbohydrate-binding module (CBM) coding sequences of the cellulosomes of 13 thermophilic, cellulolytic, anaerobic, ethanol-producing bacterial isolates having some variations in their growth and cellulose degradation capacities were amplified by PCR and then sequenced. The sequence analysis of the amplicons revealed that CBMs of 7 of the isolates including the isolate 7-9-1 with the highest capacity of cellulose degradation in solid medium have 100% identity in both nucleotide and amino acid sequences to CipB of Clostridium thermocellum in the compared regions. On the other hand, CBM of the isolate 7-1-2, also having a high cellulolytic activity, was found to differ for as much as 66 amino acid residues out of 100 (66%). The isolate 7-9-4 with a relatively low cellulose-degrading capacity also displayed amino acid variation for this protein, but only for 4 out of 118 residues.
Anahtar Kelime: cellulose cellulose digestion binding sites Clostridium thermocellum cellulolytic microorganisms polymerase chain reaction thermophilic bacteria degradation DNA sequencing carbohydrates

Konular: Biyoloji
Belge Türü: Makale Makale Türü: Araştırma Makalesi Erişim Türü: Erişime Açık
  • 1. Shoham Y, Lamed R, Bayer EA. The cellulosome concept as an efficient microbial strategy for the degradation of insoluble polysaccharides. Trends Microbiol. 7: 275-281, 1999. 2. Schwarz WH. The cellulosome and cellulose degradation by anaerobic bacteria. Appl Microbiol Biotechnol 56: 634-649, 2001. 3. Doi RH, Kosugi A, Murashima K et al. SO Cellulosomes from mesophilic bacteria. J Bacteriol 185: 5907-5914, 2003. 4. Bayer EA, Belaich J-P, Shoham Y et al. The cellulosomes: multienzyme machines for degradation of plant cell wall polysaccharides. Annu Rev Microbiol 58: 521-554, 2004. 5. Gilkes NR, Warren RAJ, Miller RC et al. Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis. J Biol Chem 263: 10401-10407, 1998. 6. Tomme P, Van Tilbeurgh H, Pettersson G et al. Studies on the cellulolytic system of Trichoderma reese/QM9414. Eur Biochem 170: 575-581, 1988. 7. Irwin D, Jung E, Wilson D. Characterization of Thermomonospora fusca xylanase. Appl Environ Microbiol 60: 763-770, 1994. 8. Reinikainen T, Rouhonen L, Nevanen T et al. Investigation of the function of mutated cellulose-binding domains of Trichoderma reesei. Proteins 14: 475-482, 1992. 9. Reinikainen T, Teleman 0, Teeri TT. Effects of pH and high ionic strength on the adsorption and activity of native and mutated cellobiohydrolase I from Trichoderma reesei. Proteins 22: 392- 403,1995. 10. Stahlberg J, Johansson G, Pettersson G. Trichoderma reesei has no true exo-cellulase: all intact and truncated cellulases produce new reducing end groups on cellulose. Biochym Biophys Acta 1157: 107-113, 1993. 11. Srisodsuk M, Lehtiö J, Under M et al. Trichoderma reesei cellobiohydrolase I with an endoglucanase cellulose-binding domain: action on microcrystalline cellulose. J. Biotechnol 57: 49- 57, 1997. 12. Glazer AN, Nikaido H. In: Microbial Biotechnology. Freeman and Company (Eds.), New York; 1995.
  • 13. Bhat MK, Bhat S. Cellulose degrading enzymes and their potential industrial applications. Biotechnol Advan 15:583, 1997. 14. Under M, Teeri TT. The roles and function of cellulose-binding domains. J Biotechnol 57: 15, 1997. 15. Tsoi TV, ChuviPskaya A, Atakishieva Ya. Yu et al. Clostridium thermocellum-a new object of genetic studies. Molekulyarnaya Genetika, Mikrobiologiya i Virusologiya 11: 18-23, 1987. 16. Hintermann G, Crameri R, Kieser T et al. Restriction analysis of the Streptomyces giaucescens genome by agarose gel electrophoresis. Arch Microbiol 130: 218-222, 1981. 17. Morag E, Lapidot A, Govorko D et al. Expression, purification and characterization of the cellulose-binding domain of the scaffolding subunit from the cellulosome of Clostridium thermocellum. Appl Environ Microbiol 61: 1980-1986, 1995. 18. Altschul SF, Gish W, Miller W et al. Basic local alignment search tool. J Mol Biol 215: 403-410, 1990. 19. Bayer EA, Morag E, Lamed R et al. Cellulosome structure: Four- pronged attack using biochemistry, molecular biology, crystallography and bioinformatics. In Charbohydrases from Trichoderma reesei and Other Microorganisms, Claeyssens, M., Nerinckx, W., and Piens, K., (Eds.) pp. 39-67. The Royal Society of Chemistry, London; 1998. 20. Bayer EA, Shimon LJW, Shoham Y et al. Cellulosomes-structure and ultrastructure. J Structural Biol 124:221-234, 1999. 21. Kataeva IA, Ronald D, Seidel III et al. Properties and mutation analysis of the CelK cellulose-binding domain from the Clostridium thermocellum cellulosome. J Biotechnol 183: 1552- 1559,2001. 22. Ozkan M, Desai SG, Zhang Y et al. Characterization of thirteen newly isolated strains of anaerobic, cellulolytic, thermophilic bacteria. Journal of Industrial Microbiology and Biotechnology 27:275-280,2001. 23. Rainey FA, Ward NL, Morgan HW et al. Phylogenetic analysis of anaerobic thermophilic bacteria: aid for their reclassification. J Bacteriol 175: 4772-4779, 1993.
APA ÖZKAN M, ÖZCENGİZ G (2006). Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates. , 45 - 50.
Chicago ÖZKAN Melek,ÖZCENGİZ Gülay Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates. (2006): 45 - 50.
MLA ÖZKAN Melek,ÖZCENGİZ Gülay Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates. , 2006, ss.45 - 50.
AMA ÖZKAN M,ÖZCENGİZ G Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates. . 2006; 45 - 50.
Vancouver ÖZKAN M,ÖZCENGİZ G Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates. . 2006; 45 - 50.
IEEE ÖZKAN M,ÖZCENGİZ G "Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates." , ss.45 - 50, 2006.
ISNAD ÖZKAN, Melek - ÖZCENGİZ, Gülay. "Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates". (2006), 45-50.
APA ÖZKAN M, ÖZCENGİZ G (2006). Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates. Turkish Journal of Biology, 30(1), 45 - 50.
Chicago ÖZKAN Melek,ÖZCENGİZ Gülay Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates. Turkish Journal of Biology 30, no.1 (2006): 45 - 50.
MLA ÖZKAN Melek,ÖZCENGİZ Gülay Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates. Turkish Journal of Biology, vol.30, no.1, 2006, ss.45 - 50.
AMA ÖZKAN M,ÖZCENGİZ G Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates. Turkish Journal of Biology. 2006; 30(1): 45 - 50.
Vancouver ÖZKAN M,ÖZCENGİZ G Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates. Turkish Journal of Biology. 2006; 30(1): 45 - 50.
IEEE ÖZKAN M,ÖZCENGİZ G "Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates." Turkish Journal of Biology, 30, ss.45 - 50, 2006.
ISNAD ÖZKAN, Melek - ÖZCENGİZ, Gülay. "Primary structure of the carbohydrate-binding modules in various cellulolytic, thermophilic, Anaerobic, Ethanol-Producing isolates". Turkish Journal of Biology 30/1 (2006), 45-50.