Effects of Carbon Sources and Various Chemicals on the Production of a Novel Amylase from a Thermophilic Bacillus sp. K-12

The amylase producer thermophilic Bacillus sp. K-12 was isolated from soil samples from Zeytinli hot spring in Kahramanmaraş. Enzyme synthesis occurred at 20-55 ºC with an optimum of 42 ºC. There was a slight variation in amylase synthesis within the pH range 4.5-10.5. Effects of various carbon sources and chemicals on a-amylase production were examined and maximum a-amylase production was obtained in a medium containing 1% starch in 60 h. MnSO4, ZnSO4 and EDTA inhibited a-amylase production of Bacillus sp. K-12.
Anahtar Kelimeler:

Thermostable, Amylase, Bacillus

Effects of Carbon Sources and Various Chemicals on the Production of a Novel Amylase from a Thermophilic Bacillus sp. K-12

The amylase producer thermophilic Bacillus sp. K-12 was isolated from soil samples from Zeytinli hot spring in Kahramanmaraş. Enzyme synthesis occurred at 20-55 ºC with an optimum of 42 ºC. There was a slight variation in amylase synthesis within the pH range 4.5-10.5. Effects of various carbon sources and chemicals on a-amylase production were examined and maximum a-amylase production was obtained in a medium containing 1% starch in 60 h. MnSO4, ZnSO4 and EDTA inhibited a-amylase production of Bacillus sp. K-12.

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  • Aira S, Kilal K, Imanaka A. Cloning and expression of thermostable α-amylase gene from Bacillus stearothermophilus in Bacillus stearothermophilus and Bacillus subtilis. Appl Environ Microbiol, 1059-1065, 1983.
  • Albayrak N, Donmez S, Balk M. Toprak ve su örneklerinden amilolitik bakterilerin izolasyonıu ve bazı enzimatik özelliklerinin belirlenmesi. Tr. J. of Biology, 20: 47-54, 1996.
  • Bernfeld P. Amylases αand β. Methods Enzymol, 1: 149-158, 1955.
  • Lowry OH, Rosebrough NJ, Forr AC et al. Protein measurement with the folin phenol reagent. J. Biol. Chem, 193: 265-275, 1951.
  • Arikan B, Unaldi N, Coral G et al. Enzymatic properties of novel thermostable, thermophilic, alkaline and chelator resistant amylase from an alkaliphilic Bacillus sp. isolate ANT-6. Process Biochemistry, 38: 1397-1403, 2003.
  • Aunstrup K. Production, isolation and economics of extracellular enzymes, In. Wingard JR, Kattchalski-Katzir LB, Golstein L (Eds.). Enzyme Technology, Appl Biochem Bieoeng, vol. 2, Academic Press, NY/San Francisco/London, 1979.
  • Uhlig H. Industrial Enzymes and their Application. PhD, Translated and Updated by Elfride M. Linsmaier-Bednar, Wiley, 1998.
  • Leveue E, Janacek S, Haye B et al. Thermophilic archeal amylolytic enzymes. Trends in Biotechnol, 7: 49-53, 1989.
  • Teodoro CES, Martins MLL. Culture conditions for the production of thermostable amylases by Bacillus sp. Brazilian Journal of Microbiology, 31: 1-9, 2000.
  • Sarıkaya E. α-Amilaz üreten bazı Bacillus sufllarının geliflme parametreleri, enzim özellik ve üretim koflullarının optimizasyonu, PhD Ankara Üniversitesi Fen Bilimleri Enstitüsü, 1995.
  • Kadrekar SN, Ramasarma GB. Amylase and protease production by Bacillus subtilis: Studies on improvement of strain and medium. J. Fd. Sci. Technol, 27: 4-6, 1990.
  • Aguilar G, Guyot MJ, Aguilar TB et al. Purification and characterization of an extracellular a-amilase produced by Lactobacillus manihotivorans LMG 18010T amylolytic lactic acid bacterium. Enzyme and Microbial Technology, 27: 406-413, 2000.
  • Sahatta AM, El-Hamahmy AF, Ahmed FH et al. The influence of certain nutritional and environmental factors on the production of amylase enzyme byStreptomyces aureofaciens 77. Journal of Islamic Academy of Sciences, 3:2, 134-138, 1990.
  • Igarashi K, Hatada Y, Hagihara H et al. Enzymatic properties of a novel liquefying α-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences. Appl Environ Microbiol, 64: 9, 3282-3289, 1998.
  • Mamo G, Gessesse A. Purification and characterization of two raw-starch-digesting thermostable α-amylase from a thermophilic Bacillus. Enzyme Microb Technol, 25: 433-8, 1999.
  • Aboud-zeid AM. Production and characterization of an extracellular α-amylase enzyme from Aspergillus flavus. Microbios. 89: 55-66, 1997.
  • Özcelik S. Genel Mikrobiyoloji Uygulama Kılavuzu. Süleyman Demirel Üniversitesi Ziraat Fakültesi Yayınları No.2, 92s, 1995.
  • Horikoshi K. Alkaliphiles–from an industrial point of view. FEMS Microbiology Reviews, 18: 259-270, 1996.
  • Oxaki A, Tanaka A. Heat stable alkaline amylase from Bacillus. Japanase Kokai Patent, 9, 049, 584, 1990.