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Yıl 2022, , 30 - 35, 28.12.2022

Dilsat Nigar Colak

https://doi.org/10.46810/tdfd.1169601

Öz

Kaynakça

  • [1] Li S, Yang X, Yang S, Zhu M, Wang X. Technology prospecting on enzymes: application, marketing and engineering. Comput. Struct. Biotechnol. J. 2012;2:1–11.
  • [2] Gomes I, Gomes J, Steiner W. Highly thermostable amylase and pullulanase of the extreme thermophilic eubacterium Rhodothermus marinus: production and partial characterization. Bioresour. Technol. 2003;90 (2);207-214.
  • [3] Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37;233–238.
  • [4] Nagano N, Orengo C.A, Thornton JM. One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J. Mol. Biol. 2002;321;741-765.
  • [5] Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B. Microbial α-amylases: a biotechnological perspective. Process Biochem. 2003;38;1599 – 1616.
  • [6] Ma Y, Yang H, Chen X, Sun B, Du G, Zhou Z, et al. Significantly improving the yield of recombinant proteins in Bacillus subtilis by a novel powerful mutagenesis tool (ARTP): Alkaline α-amylase as a case study. Protein Express. Purif. 2015;114;82-88.
  • [7] Shafiei M, Ziaee AA, Amoozegar MA. Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. strain F. J. Ind. Microbiol. Biotechnol. 2011;38;275–81.
  • [8] Hussain I, Siddique F, Mahmood MS, Ahmed SI. A Review of the Microbiological Aspect of α-amylase Production. IJAB. 2013;15(5);1029-1034.
  • [9] Sundarram A, Murthy TPK. α-Amylase production and applications: a review. J. Appl. Environ. Microbiol. 2014; 2;166-175.
  • [10] Collins MD, Brown J, Jones D. Brachybacterium faeciumgen. nov., sp. nov., a coryneform bacterium from poultry litter. Int. J. Syst. Bacteriol. 1988;38; 45–48.
  • [11] Lapidus A, Pukall R, Labuttii K, Copeland A, Glavina Del Rio T, Nolan M, et al. Complete genome sequence of Brachybacterium faecium type strain (Schefferle 6-10). Stand. Genomic Sci. 2009;1;3–11.
  • [12] Park SK, Kim MS, Jung MJ, Nam YD, Park EJ, Roh SW. et al. Brachybacterium squillarum sp. nov., isolated from salt-fermented seafood. Int. J. Syst. Evol. Microbiol. 2011;61;1118–1122.
  • [13] Singh H, Du J, Yang JE, Yin CS, Kook M, Yi TH. Brachybacterium horti sp. nov., isolated from garden soil. Int. J. Syst. Evol. Microbiol. 2016;66;189–195.
  • [14] Doukyu N, Yamagishi W, Kuwahara H, Ogino H, Furuki N. Purification and characterization of a maltooligosaccharide-forming amylase that improves product selectivity in water-miscible organic solvents, from dimethylsulfoxide-tolerant Brachybacterium sp. strain LB25. Extremophiles. 2007;11;781–788.
  • [15] Atlas RM, Parks LC, Brown AE. Laboratory Manual of Experimental Microbiology. St Louis: Mosby-Year Book Inc.; 1995.
  • [16] Bernfeld P. Amylases, α and β. Methods. Enzymol. 1955;1;149–158.
  • [17] Bradford MM. A rapid and sensitive method for the quantitation of microgram quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976;72;248-254.
  • [18] Mageswari A, Subramanian P, Chandrasekaran S, Sivashanmugam K, Babu S, Gothandam KM. Optimization and immobilization of amylase obtained from halotolerant bacteria isolated from solar salterns. J. Genet. Eng. Biotechnol. 2012;10(2);201-8.
  • [19] Konsoula Z, Liakopoulou-Kyriakides M. Co-production of alpha-amylase and beta-galactosidase by Bacillus subtilis in complex organic substrates. Bioresour. Technol. 2007;98;150–157.
  • [20] Souza PMD, Pérola OM. Application of Microbial α-Amylase in Industry-A Review. Braz. J. Microbiol. 2010;41;850-861.
  • [21] Doukyu N, Yamagishi W, Kuwahara H, Ogino H. A Maltooligosaccharide-Forming Amylase Gene from Brachybacterium sp. Strain LB25: Cloning and Expression in Escherichia coli. Biosci. Biotechnol. Biochem. 2008;72(9);2444–2447.
  • [22] Farooq MA., Ali S, Hassan A, Tahir HM, Mumtaz S, Mumtaz S. Biosynthesis and industrial applications of α‑amylase: a review. Arch. Microbiol. 2021;203;1281–1292.
  • [23] Mehta D, Satyanarayana T. Bacterial and archaeal α-amylases: diversity and amelioration of the desirable characteristics for industrial applications. Front. Microbiol. 2016;7;1129.
  • [24] Yildirim Akatın M. An Overview of Amylase Production by Solid State Fermentation (SSF) since 2010. JTST. 2019;9(1);1-7.
  • [25] Aiyer PV. Amylases and their applications. Afr. J. Biotechnol. 2005;4 (13);1525-1529.
  • [26] Acer O, Pirinccioglu H, Bekler FM, Gul-Guven R, Güven K. Anoxybacillus sp. AH1, an α-amylase-producing thermophilic bacterium isolated from Dargecit Hot Spring. Biologia. 2015;70(7);853-862.
  • [27] Ozdemir S, Okumus V, Ulutas MS, Dundar A, Akarsubası AT, et al. Isolation of a Novel Thermophilic Anoxybacillus flavithermus SO-13, Production, Characterization and Industrial Applications of its Thermostable α-Amylase. J. Bioprocess Biotech. 2015;5;237.
  • [28] Sharma N, Vamil R, Ahmad S, Agarwal R. Effect of Different Carbon and Nitrogen Sources on Α- Amylase Production from Bacıllus Amylolıquefacıens. IJPSR. 2012;3(4);1161-1163.
  • [29] Fincan SA, Enez B, Ozdemir S, Bekler FM. Purification and characterization of thermostable a-amylase from thermophilic Anoxybacillus flavithermus. Carbohydr. Polym. 2014;102;144-150.
  • [30] Singh R, Kapoor V, Kumar V. Influence of Carbon and Nitrogen Sources on the α-amylase Production by a Newly Isolated thermophilic Streptomyces sp. MSC702 (MTCC 10772). Asian J. Biotechnol. 2011;3;540-553.
  • [31] Lall BM, Paul JS, Jadav SK, Tiwari KL. Effect of Carbon and Nitrogen Source α-Amylase Enzyme Production from Bacillus Subtilis MB6. Indian J. Aerobiol. 2016;29;37-41.
  • [32] Qader SAU, Bano S, Aman A, Syed N, Azhar AA. Enhanced productionand extracellular activity of commercially important amylolytic enzyme by anewly isolated strain of Bacillus sp. AS-1. TJB. 2006;31;135–140.

Isolation of a Novel Amylase Producing Brachybacterium paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions

Yıl 2022, , 30 - 35, 28.12.2022

Dilsat Nigar Colak

https://doi.org/10.46810/tdfd.1169601

Öz

A novel amylase producing bacterium FAD4 was isolated from the wastewater of a textile factory located in Soke (Aydın/Turkey). The amylase production ability of gram positive, coccoidal FAD4 strain was confirmed with plate assay. Morphological and 16S rRNA sequence analyses revealed that FAD4 belongs to the Brachybacterium paraconglomeratum species with a sequence similarity of 99.8%. The optimal conditions for amylase production were determined as 72 h at 30 °C with supplementation of 1% starch. Optimum temperature and pH of the amylase were 50 °C and 7.0 respectively. Different starch, carbon and nitrogen sources were investigated for amylase production. A high enzyme production was observed with 1% potato starch and among nitrogen sources peptone was induced the production of amylase. Lactose, galactose, and fructose were also increased the enzyme production as carbon sources.

Anahtar Kelimeler

Amylase Brachybacterium starch

Kaynakça

  • [1] Li S, Yang X, Yang S, Zhu M, Wang X. Technology prospecting on enzymes: application, marketing and engineering. Comput. Struct. Biotechnol. J. 2012;2:1–11.
  • [2] Gomes I, Gomes J, Steiner W. Highly thermostable amylase and pullulanase of the extreme thermophilic eubacterium Rhodothermus marinus: production and partial characterization. Bioresour. Technol. 2003;90 (2);207-214.
  • [3] Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37;233–238.
  • [4] Nagano N, Orengo C.A, Thornton JM. One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J. Mol. Biol. 2002;321;741-765.
  • [5] Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B. Microbial α-amylases: a biotechnological perspective. Process Biochem. 2003;38;1599 – 1616.
  • [6] Ma Y, Yang H, Chen X, Sun B, Du G, Zhou Z, et al. Significantly improving the yield of recombinant proteins in Bacillus subtilis by a novel powerful mutagenesis tool (ARTP): Alkaline α-amylase as a case study. Protein Express. Purif. 2015;114;82-88.
  • [7] Shafiei M, Ziaee AA, Amoozegar MA. Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. strain F. J. Ind. Microbiol. Biotechnol. 2011;38;275–81.
  • [8] Hussain I, Siddique F, Mahmood MS, Ahmed SI. A Review of the Microbiological Aspect of α-amylase Production. IJAB. 2013;15(5);1029-1034.
  • [9] Sundarram A, Murthy TPK. α-Amylase production and applications: a review. J. Appl. Environ. Microbiol. 2014; 2;166-175.
  • [10] Collins MD, Brown J, Jones D. Brachybacterium faeciumgen. nov., sp. nov., a coryneform bacterium from poultry litter. Int. J. Syst. Bacteriol. 1988;38; 45–48.
  • [11] Lapidus A, Pukall R, Labuttii K, Copeland A, Glavina Del Rio T, Nolan M, et al. Complete genome sequence of Brachybacterium faecium type strain (Schefferle 6-10). Stand. Genomic Sci. 2009;1;3–11.
  • [12] Park SK, Kim MS, Jung MJ, Nam YD, Park EJ, Roh SW. et al. Brachybacterium squillarum sp. nov., isolated from salt-fermented seafood. Int. J. Syst. Evol. Microbiol. 2011;61;1118–1122.
  • [13] Singh H, Du J, Yang JE, Yin CS, Kook M, Yi TH. Brachybacterium horti sp. nov., isolated from garden soil. Int. J. Syst. Evol. Microbiol. 2016;66;189–195.
  • [14] Doukyu N, Yamagishi W, Kuwahara H, Ogino H, Furuki N. Purification and characterization of a maltooligosaccharide-forming amylase that improves product selectivity in water-miscible organic solvents, from dimethylsulfoxide-tolerant Brachybacterium sp. strain LB25. Extremophiles. 2007;11;781–788.
  • [15] Atlas RM, Parks LC, Brown AE. Laboratory Manual of Experimental Microbiology. St Louis: Mosby-Year Book Inc.; 1995.
  • [16] Bernfeld P. Amylases, α and β. Methods. Enzymol. 1955;1;149–158.
  • [17] Bradford MM. A rapid and sensitive method for the quantitation of microgram quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976;72;248-254.
  • [18] Mageswari A, Subramanian P, Chandrasekaran S, Sivashanmugam K, Babu S, Gothandam KM. Optimization and immobilization of amylase obtained from halotolerant bacteria isolated from solar salterns. J. Genet. Eng. Biotechnol. 2012;10(2);201-8.
  • [19] Konsoula Z, Liakopoulou-Kyriakides M. Co-production of alpha-amylase and beta-galactosidase by Bacillus subtilis in complex organic substrates. Bioresour. Technol. 2007;98;150–157.
  • [20] Souza PMD, Pérola OM. Application of Microbial α-Amylase in Industry-A Review. Braz. J. Microbiol. 2010;41;850-861.
  • [21] Doukyu N, Yamagishi W, Kuwahara H, Ogino H. A Maltooligosaccharide-Forming Amylase Gene from Brachybacterium sp. Strain LB25: Cloning and Expression in Escherichia coli. Biosci. Biotechnol. Biochem. 2008;72(9);2444–2447.
  • [22] Farooq MA., Ali S, Hassan A, Tahir HM, Mumtaz S, Mumtaz S. Biosynthesis and industrial applications of α‑amylase: a review. Arch. Microbiol. 2021;203;1281–1292.
  • [23] Mehta D, Satyanarayana T. Bacterial and archaeal α-amylases: diversity and amelioration of the desirable characteristics for industrial applications. Front. Microbiol. 2016;7;1129.
  • [24] Yildirim Akatın M. An Overview of Amylase Production by Solid State Fermentation (SSF) since 2010. JTST. 2019;9(1);1-7.
  • [25] Aiyer PV. Amylases and their applications. Afr. J. Biotechnol. 2005;4 (13);1525-1529.
  • [26] Acer O, Pirinccioglu H, Bekler FM, Gul-Guven R, Güven K. Anoxybacillus sp. AH1, an α-amylase-producing thermophilic bacterium isolated from Dargecit Hot Spring. Biologia. 2015;70(7);853-862.
  • [27] Ozdemir S, Okumus V, Ulutas MS, Dundar A, Akarsubası AT, et al. Isolation of a Novel Thermophilic Anoxybacillus flavithermus SO-13, Production, Characterization and Industrial Applications of its Thermostable α-Amylase. J. Bioprocess Biotech. 2015;5;237.
  • [28] Sharma N, Vamil R, Ahmad S, Agarwal R. Effect of Different Carbon and Nitrogen Sources on Α- Amylase Production from Bacıllus Amylolıquefacıens. IJPSR. 2012;3(4);1161-1163.
  • [29] Fincan SA, Enez B, Ozdemir S, Bekler FM. Purification and characterization of thermostable a-amylase from thermophilic Anoxybacillus flavithermus. Carbohydr. Polym. 2014;102;144-150.
  • [30] Singh R, Kapoor V, Kumar V. Influence of Carbon and Nitrogen Sources on the α-amylase Production by a Newly Isolated thermophilic Streptomyces sp. MSC702 (MTCC 10772). Asian J. Biotechnol. 2011;3;540-553.
  • [31] Lall BM, Paul JS, Jadav SK, Tiwari KL. Effect of Carbon and Nitrogen Source α-Amylase Enzyme Production from Bacillus Subtilis MB6. Indian J. Aerobiol. 2016;29;37-41.
  • [32] Qader SAU, Bano S, Aman A, Syed N, Azhar AA. Enhanced productionand extracellular activity of commercially important amylolytic enzyme by anewly isolated strain of Bacillus sp. AS-1. TJB. 2006;31;135–140.
Toplam 32 adet kaynakça vardır.

Ayrıntılar

Birincil Dil İngilizce
Bölüm Makaleler
Yazarlar

Dilsat Nigar Colak 0000-0001-9544-3733

Yayımlanma Tarihi 28 Aralık 2022
Yayımlandığı Sayı Yıl 2022

Kaynak Göster

APA Colak, D. N. (2022). Isolation of a Novel Amylase Producing Brachybacterium paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions. Türk Doğa Ve Fen Dergisi, 11(4), 30-35. https://doi.org/10.46810/tdfd.1169601
AMA Colak DN. Isolation of a Novel Amylase Producing Brachybacterium paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions. TDFD. Aralık 2022;11(4):30-35. doi:10.46810/tdfd.1169601
Chicago Colak, Dilsat Nigar. “Isolation of a Novel Amylase Producing Brachybacterium Paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions”. Türk Doğa Ve Fen Dergisi 11, sy. 4 (Aralık 2022): 30-35. https://doi.org/10.46810/tdfd.1169601.
EndNote Colak DN (01 Aralık 2022) Isolation of a Novel Amylase Producing Brachybacterium paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions. Türk Doğa ve Fen Dergisi 11 4 30–35.
IEEE D. N. Colak, “Isolation of a Novel Amylase Producing Brachybacterium paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions”, TDFD, c. 11, sy. 4, ss. 30–35, 2022, doi: 10.46810/tdfd.1169601.
ISNAD Colak, Dilsat Nigar. “Isolation of a Novel Amylase Producing Brachybacterium Paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions”. Türk Doğa ve Fen Dergisi 11/4 (Aralık 2022), 30-35. https://doi.org/10.46810/tdfd.1169601.
JAMA Colak DN. Isolation of a Novel Amylase Producing Brachybacterium paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions. TDFD. 2022;11:30–35.
MLA Colak, Dilsat Nigar. “Isolation of a Novel Amylase Producing Brachybacterium Paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions”. Türk Doğa Ve Fen Dergisi, c. 11, sy. 4, 2022, ss. 30-35, doi:10.46810/tdfd.1169601.
Vancouver Colak DN. Isolation of a Novel Amylase Producing Brachybacterium paraconglomeratum Strain FAD4 and Optimization of the Enzyme Production Conditions. TDFD. 2022;11(4):30-5.

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