Araştırma Makalesi
BibTex RIS Kaynak Göster
Yıl 2022, Cilt: 11 Sayı: 4, 36 - 41, 28.12.2022
https://doi.org/10.46810/tdfd.1170755

Öz

Kaynakça

  • [1] Sun L, Warren FJ, Gidley MJ. Natural products for glycaemic control: Polyphenols as inhibitors of alpha-amylase. Trends Food Sci Technol. 2019; 91:262-273.
  • [2] Sundarram A, Murthy TPK. α-amylase production and applications: a review. J Appl Environment Microbiol. 2014;2(4):166-175.
  • [3] Abou-Elela GM, El-Sersy NA, Wefky SH. Statistical optimization of cold adapted α-amylase production by free and immobilized cells of Nocardiopsis aegyptia. J Appl Sci Res. 2009;5(3):286-292.
  • [4] 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(4)1281-1292.
  • [5] Papoutsis K, Zhang J, Bowyer MC, Brunton N, Gibney ER, Lyng J. Fruit, vegetables, and mushrooms for the preparation of extracts with α-amylase and α-glucosidase inhibition properties: A review. Food Chem. 2021;338: 128119.
  • [6] Zheng Y, Tian J, Yang W, Chen S, Liu D, Fang H, Ye X. Inhibition mechanism of ferulic acid against α-amylase and α-glucosidase. Food Chem. 2020;317:126346.
  • [7] Far BE, Ahmadi Y, Khosroshahi AY, Dilmaghani A. Microbial alpha-amylase production: progress, challenges and perspectives. Advance Pharma Bull. 2020;10(3):350.
  • [8] Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B. Microbial α-Amylase: a Biotechnological Perspective. Process Biochem. 2003;1-18.
  • [9] Agüloğlu Fincan S, Özdemir S, Karakaya A, Enez B, Demiroğlu Mustafov S, Ulutaş MS, Şen, F. Purification and characterization of thermostable α-amylase produced from Bacillus licheniformis So-B3 and its potential in hydrolyzing raw starch. Life Sci. 2021;1:264.
  • [10] Woodley JM. Advances in enzyme technology-UK Contributions.(Th.scheperi editör). Advance Biochem Eng/Biotechnol, Springer-Verlag. Berlin Heidelberg. 2000;94.
  • [11] Agüloğlu S, Ensari NY, Uyar F, Otludil B. The effects of amino acids on production and transport of -amylase through bacterial membranes. Starch/Starke, 2000;52, 290-295.
  • [12] Du R, Zhao F, Qiao X, Song Q, Ye G, Wang Y, Wang B, Han Y, Zhou Z. Optimization and partial characterization of ca-independent α-amylase from Bacillus amyloliquefaciens BH1, Prep Biochem Biotechnol.2018;48(8):768–774.
  • [13] Enez B.Purification and Characterization of Thermostable α-Amylase from Soil Bacterium Bacillus sp.Prot. Peptid Let. 2021;28(12):1372-1378.
  • [14] John RJD, Elangovan N. Molecular identification of amylase producing Bacillus subtilis and detection of optimal conditions. J Pharm Res 2013;6: 426-30.
  • [15] De Vos P. et al. Bergey's Manual of 1.Systematic Bacteriology: Volume 3: The Firmicutes. Springer, 2009.
  • [16] Vary PS, Biedendieck R, Fuerch T, Meinhardt F, Rohde M, Deckwer WD, Jahn D. (). Bacillus megaterium — from simple soil bacterium to industrial protein production host. Appl Microb Biotechnol. 2007;76: 957–967.
  • [17] Bunk B, Schulz A, Stammen S, et al. A short story about a big magic bug Boyke. Bioengineered Bugs. 2010; 1(2):85-91.
  • [18] Simair AA, Khushk I, Qureshi AS, Bhutto MA, Chaudhry HA, Ansari KA, Lu C. (). Amylase production from thermophilic Bacillus sp. BCC 021-50 isolated from a marine environment. Fermentation, 2017;3(2):25.
  • [19] Lowry OH, Rosebrough NJ, Farr AL. et al. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951;193:265-275.
  • [20] Bernfeld P. Enzymes carbohydrate metabolism, ln Methods ln Enzymology, Academic Press. 1955;17:149-158.
  • [21] Özdemir S, Agüloğlu Fincan S, Karakaya A, Enez B. A novel raw starch hydrolyzing thermostable α-amylase produced by newly isolated Bacillus mojavensis SO-10: purification, characterization and usage in starch industries. Brazil Arch Bio Technol. 2018: 61.
  • [22] Al-Johani NB, Al-seeni MN, Ahmed YM. Optimization of alkaline α-amylase production by thermophilic Bacillus subtilis. Afr J Trad, Compl Alternati Meedici. 2017;14(1):288-301.
  • [23] Ortakaya V, Agüloğlu Fincan S, Enez B. α-Amylase from Bacillus simplex production, characterization and partial purification. Fresenius Environ Bull. 2017;26:4446–4455.
  • [24] Agüloğlu Fincan S, Enez B. Production, purification, and characterization of thermostable α-amylase from thermophilic Geobacillus stearothermophilus, Starch/Stärke. 2014;66:182-189.
  • [25] Rakaz MA, Hussien MO, Ibrahim HM. Isolation, Extraction, Purification, and Molecular Characterization for Thermostable α-Amylase from Locally Isolated Bacillus Species in Sudan. Biochemistry Res Int. 2021: 6670380.
  • [26] Kannan TR, Kanagaraj C. Molecular characteristic of α-amylase enzymes producing from Bacillus lichenformis (JQ946317) using solid state fermentation. Biocatal Agri Biotechnol. 2019;20:101240.
  • [27] Najafi MF, Deobagkar D, Deobagkar D. Purification and characterization of an extracellular α-amylase from Bacillus subtilis AX20. Protein Expr Purif. 2005;41:349–354.
  • [28] Behal A, Sınghj J, Sharma MK, Puri P, Batra N. Characterization of alkaline α-amylase from Bacillus sp. AB04. Int J Agri Biol. 2006; 8: 80–83.
  • [29] Saxena RK, Dutt K, Agarwal L, Nayyar P. A highly thermostable and alkaline amylase from a Bacillus sp. PN5. Biores Technol. 2007;98: 260–265.
  • [30] Carvalho RV, Cõrrea TLR, Silva JCM, Mansur LRCO, Martins MLL. Properties of an amylase from thermophilic Bacillus sp., Brazil J Microbiol. 2008; 39: 102–107.
  • [31] Prakash B, Vidyasagar M, Madhukumar MS, Muralikrishna G, Sreeramulu K. Production, purification, and characterization of two extremely halotolerant thermostable, and alkali-stable α-amylases from Chromohalobacter sp. TVSP 101. Process Biochem. 2009; 44:210–215.
  • [32] Asgher M, Javaid Asad M, Rahman SU, Legge RL. A thermostable α-amylase from a moderately thermophilic Bacillus subtilis strain for starch processing. J Food Eng. 2007; 79: 950–955.

Production of α-Amylase from Bacillus megaterium MD-1

Yıl 2022, Cilt: 11 Sayı: 4, 36 - 41, 28.12.2022
https://doi.org/10.46810/tdfd.1170755

Öz

The alpha-amylase is used extensively in many different industrial sectors and is renowned for modifying starch by rupturing 1-4 glycosidic bands. Depending on the intrinsic properties of the microorganism, several alpha-amylases with thermostable and halotolerant properties are expressed. In the current study, the bacteria were isolated from Ergani Makam Mountain. Identification and optimization of the isolated bacteria were performed. As a result of the 16S rRNA analysis, physiological, morphological and biochemical analyis were carried out for the identification of the isolated microorganism and consequently the bacterium was defined as Bacillus megaterium MD-1.
Following its identification, α-Amylase, was isolated from B. megaterium. Optimal conditions for bacteria and enzyme production were determined as 48 hours, 35°C and pH 7.0. Maximum enzyme activity was optained at 40°C and pH 8.0. The effects of various carbon and nitrogen sources on enzyme production were investigated by adding to the nutrient medium. Compared to the control regarding enzyme production, it was determined that carbon sources, particularly sucrose, fructose and lactose inhibited enzyme production by 75%, no change on the other hand was observed in glucose, starch and galactose. It was also observed that urea and sodium nitrate from nitrogen sources had an inhibitory effect on enzyme production whereas other nitrogen sources did not. The highest amylase production among nitrogen sources was obtained with peptone addition.
In our study, it was determined that an increase in amylase activity could be achieved by using the optimum values of physical parameters.

Kaynakça

  • [1] Sun L, Warren FJ, Gidley MJ. Natural products for glycaemic control: Polyphenols as inhibitors of alpha-amylase. Trends Food Sci Technol. 2019; 91:262-273.
  • [2] Sundarram A, Murthy TPK. α-amylase production and applications: a review. J Appl Environment Microbiol. 2014;2(4):166-175.
  • [3] Abou-Elela GM, El-Sersy NA, Wefky SH. Statistical optimization of cold adapted α-amylase production by free and immobilized cells of Nocardiopsis aegyptia. J Appl Sci Res. 2009;5(3):286-292.
  • [4] 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(4)1281-1292.
  • [5] Papoutsis K, Zhang J, Bowyer MC, Brunton N, Gibney ER, Lyng J. Fruit, vegetables, and mushrooms for the preparation of extracts with α-amylase and α-glucosidase inhibition properties: A review. Food Chem. 2021;338: 128119.
  • [6] Zheng Y, Tian J, Yang W, Chen S, Liu D, Fang H, Ye X. Inhibition mechanism of ferulic acid against α-amylase and α-glucosidase. Food Chem. 2020;317:126346.
  • [7] Far BE, Ahmadi Y, Khosroshahi AY, Dilmaghani A. Microbial alpha-amylase production: progress, challenges and perspectives. Advance Pharma Bull. 2020;10(3):350.
  • [8] Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B. Microbial α-Amylase: a Biotechnological Perspective. Process Biochem. 2003;1-18.
  • [9] Agüloğlu Fincan S, Özdemir S, Karakaya A, Enez B, Demiroğlu Mustafov S, Ulutaş MS, Şen, F. Purification and characterization of thermostable α-amylase produced from Bacillus licheniformis So-B3 and its potential in hydrolyzing raw starch. Life Sci. 2021;1:264.
  • [10] Woodley JM. Advances in enzyme technology-UK Contributions.(Th.scheperi editör). Advance Biochem Eng/Biotechnol, Springer-Verlag. Berlin Heidelberg. 2000;94.
  • [11] Agüloğlu S, Ensari NY, Uyar F, Otludil B. The effects of amino acids on production and transport of -amylase through bacterial membranes. Starch/Starke, 2000;52, 290-295.
  • [12] Du R, Zhao F, Qiao X, Song Q, Ye G, Wang Y, Wang B, Han Y, Zhou Z. Optimization and partial characterization of ca-independent α-amylase from Bacillus amyloliquefaciens BH1, Prep Biochem Biotechnol.2018;48(8):768–774.
  • [13] Enez B.Purification and Characterization of Thermostable α-Amylase from Soil Bacterium Bacillus sp.Prot. Peptid Let. 2021;28(12):1372-1378.
  • [14] John RJD, Elangovan N. Molecular identification of amylase producing Bacillus subtilis and detection of optimal conditions. J Pharm Res 2013;6: 426-30.
  • [15] De Vos P. et al. Bergey's Manual of 1.Systematic Bacteriology: Volume 3: The Firmicutes. Springer, 2009.
  • [16] Vary PS, Biedendieck R, Fuerch T, Meinhardt F, Rohde M, Deckwer WD, Jahn D. (). Bacillus megaterium — from simple soil bacterium to industrial protein production host. Appl Microb Biotechnol. 2007;76: 957–967.
  • [17] Bunk B, Schulz A, Stammen S, et al. A short story about a big magic bug Boyke. Bioengineered Bugs. 2010; 1(2):85-91.
  • [18] Simair AA, Khushk I, Qureshi AS, Bhutto MA, Chaudhry HA, Ansari KA, Lu C. (). Amylase production from thermophilic Bacillus sp. BCC 021-50 isolated from a marine environment. Fermentation, 2017;3(2):25.
  • [19] Lowry OH, Rosebrough NJ, Farr AL. et al. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951;193:265-275.
  • [20] Bernfeld P. Enzymes carbohydrate metabolism, ln Methods ln Enzymology, Academic Press. 1955;17:149-158.
  • [21] Özdemir S, Agüloğlu Fincan S, Karakaya A, Enez B. A novel raw starch hydrolyzing thermostable α-amylase produced by newly isolated Bacillus mojavensis SO-10: purification, characterization and usage in starch industries. Brazil Arch Bio Technol. 2018: 61.
  • [22] Al-Johani NB, Al-seeni MN, Ahmed YM. Optimization of alkaline α-amylase production by thermophilic Bacillus subtilis. Afr J Trad, Compl Alternati Meedici. 2017;14(1):288-301.
  • [23] Ortakaya V, Agüloğlu Fincan S, Enez B. α-Amylase from Bacillus simplex production, characterization and partial purification. Fresenius Environ Bull. 2017;26:4446–4455.
  • [24] Agüloğlu Fincan S, Enez B. Production, purification, and characterization of thermostable α-amylase from thermophilic Geobacillus stearothermophilus, Starch/Stärke. 2014;66:182-189.
  • [25] Rakaz MA, Hussien MO, Ibrahim HM. Isolation, Extraction, Purification, and Molecular Characterization for Thermostable α-Amylase from Locally Isolated Bacillus Species in Sudan. Biochemistry Res Int. 2021: 6670380.
  • [26] Kannan TR, Kanagaraj C. Molecular characteristic of α-amylase enzymes producing from Bacillus lichenformis (JQ946317) using solid state fermentation. Biocatal Agri Biotechnol. 2019;20:101240.
  • [27] Najafi MF, Deobagkar D, Deobagkar D. Purification and characterization of an extracellular α-amylase from Bacillus subtilis AX20. Protein Expr Purif. 2005;41:349–354.
  • [28] Behal A, Sınghj J, Sharma MK, Puri P, Batra N. Characterization of alkaline α-amylase from Bacillus sp. AB04. Int J Agri Biol. 2006; 8: 80–83.
  • [29] Saxena RK, Dutt K, Agarwal L, Nayyar P. A highly thermostable and alkaline amylase from a Bacillus sp. PN5. Biores Technol. 2007;98: 260–265.
  • [30] Carvalho RV, Cõrrea TLR, Silva JCM, Mansur LRCO, Martins MLL. Properties of an amylase from thermophilic Bacillus sp., Brazil J Microbiol. 2008; 39: 102–107.
  • [31] Prakash B, Vidyasagar M, Madhukumar MS, Muralikrishna G, Sreeramulu K. Production, purification, and characterization of two extremely halotolerant thermostable, and alkali-stable α-amylases from Chromohalobacter sp. TVSP 101. Process Biochem. 2009; 44:210–215.
  • [32] Asgher M, Javaid Asad M, Rahman SU, Legge RL. A thermostable α-amylase from a moderately thermophilic Bacillus subtilis strain for starch processing. J Food Eng. 2007; 79: 950–955.
Toplam 32 adet kaynakça vardır.

Ayrıntılar

Birincil Dil İngilizce
Konular Mühendislik
Bölüm Makaleler
Yazarlar

Sema Agüloğlu Fincan 0000-0003-0147-4411

Bariş Enez 0000-0003-4730-3458

Yayımlanma Tarihi 28 Aralık 2022
Yayımlandığı Sayı Yıl 2022 Cilt: 11 Sayı: 4

Kaynak Göster

APA Agüloğlu Fincan, S., & Enez, B. (2022). Production of α-Amylase from Bacillus megaterium MD-1. Türk Doğa Ve Fen Dergisi, 11(4), 36-41. https://doi.org/10.46810/tdfd.1170755
AMA Agüloğlu Fincan S, Enez B. Production of α-Amylase from Bacillus megaterium MD-1. TDFD. Aralık 2022;11(4):36-41. doi:10.46810/tdfd.1170755
Chicago Agüloğlu Fincan, Sema, ve Bariş Enez. “Production of α-Amylase from Bacillus Megaterium MD-1”. Türk Doğa Ve Fen Dergisi 11, sy. 4 (Aralık 2022): 36-41. https://doi.org/10.46810/tdfd.1170755.
EndNote Agüloğlu Fincan S, Enez B (01 Aralık 2022) Production of α-Amylase from Bacillus megaterium MD-1. Türk Doğa ve Fen Dergisi 11 4 36–41.
IEEE S. Agüloğlu Fincan ve B. Enez, “Production of α-Amylase from Bacillus megaterium MD-1”, TDFD, c. 11, sy. 4, ss. 36–41, 2022, doi: 10.46810/tdfd.1170755.
ISNAD Agüloğlu Fincan, Sema - Enez, Bariş. “Production of α-Amylase from Bacillus Megaterium MD-1”. Türk Doğa ve Fen Dergisi 11/4 (Aralık 2022), 36-41. https://doi.org/10.46810/tdfd.1170755.
JAMA Agüloğlu Fincan S, Enez B. Production of α-Amylase from Bacillus megaterium MD-1. TDFD. 2022;11:36–41.
MLA Agüloğlu Fincan, Sema ve Bariş Enez. “Production of α-Amylase from Bacillus Megaterium MD-1”. Türk Doğa Ve Fen Dergisi, c. 11, sy. 4, 2022, ss. 36-41, doi:10.46810/tdfd.1170755.
Vancouver Agüloğlu Fincan S, Enez B. Production of α-Amylase from Bacillus megaterium MD-1. TDFD. 2022;11(4):36-41.