Research Article
BibTex RIS Cite

Alpha-amylase activity of lactic acid bacteria isolated from different fermented products: Characterization of Latilactobacillus curvatus Y2-1B amylase

Year 2025, Volume: 14 Issue: 2, 64 - 72, 27.06.2025
https://doi.org/10.46810/tdfd.1619709

Abstract

In this study, ninety-one lactic acid bacteria isolates were obtained from different fermented products and their ability to produce α-amylase was qualitatively examined using starch added medium. Among the isolated strains, 75 LABs were qualitatively accepted as amylase positive and a total of 20 LABs were determined to have high α-amylase production ability and quantitative α-amylase enzyme activity studies were performed. Quantitative enzyme activity results for LABs were found in the range of 1.283 U/mL- 13.670 U/mL. Then, 3 LAB isolates (P4-2B, Y2-1B, S1-2B) were selected and identified by genotypic methods. After identification, enzyme was partially purified from Latilactobacillus curvatusY2-1B isolate and activity analyses included the effect on pH, temperature and cations were determined. The lowest enzyme activity was found to be 0.554 U/ml at the pH 9 and 0.694 U/ml at pH 6 as a highest value (p<0.05). On the other hand, the purified enzyme formed a band of approximately 40kDa in SDS-PAGE while the presence of the genes amy were examined and approved. It was thought that these selected LAB isolates may be useful in industrial biotechnology and microbial enzyme industry due to their α-amylase enzyme activity.

Supporting Institution

Erciyes University Scientific Research Projects Coordination Unit

Project Number

FYL-2021-11216

Thanks

This study was financially supported by Erciyes University Scientific Research Projects Coordination Unit under Grant number of FYL-2021-11216.

References

  • Abiodun Onilude A, Solomon Ayinla G, Eluehike C. Properties of Alpha-amylase of Lactobacillus plantarum Isolated from Cassava Waste Samples. Biotechnol J Int 2017; 19: 1–14.
  • Temel Y, Ayna A, Hamdi Shafeeq I, Ciftci M. In vitro effects of some antibiotics on glucose-6-phosphate dehydrogenase from rat (Rattus norvegicus) erythrocyte. Drug Chem Toxicol 2020; 43: 219–223.
  • Bayindir S, Ayna A, Temel Y, Ciftci M. The synthesis of new oxindoles as analogs of natural product 3,3″-bis(indolyl)oxindole and in vitro evaluation of the enzyme activity of G6PD and 6PGD. Turk J Chem 2018; 42: 332–345.
  • Bayindir S, Temel Y, Ayna A, Ciftci M. The synthesis of N‐benzoylindoles as inhibitors of rat erythrocyte glucose‐6‐phosphate dehydrogenase and 6‐phosphogluconate dehydrogenase. J Biochem Mol Toxicol 2018; 32: e22193.
  • Ataallahi E, Naderi-Manesh H, Roostaazad R, Yeganeh S. A simple 2-step purification process of α-amylase from Bacillus subtilis: Optimization by response surface methodology. Int J Biol Macromol 2021; 192: 64–71.
  • Axelsson LT. Lactic acid bacteria: classification and physiology. In: Salmina S, Wright AV, eds. Lactic Acid Bacteria. USA: Marcel Dekker Inc; 1993. p.1–63.
  • Bamigboye CO, Okonji RE, Oluremi IO, James V. Stain removing, juice-clarifying, and starch-liquefying potentials of amylase from Pleurotus tuberregium in submerged fermentation system. J Genet Eng Biotechnol 2022; 20: 23.
  • Bernfeld P. Enzymes Carbohydrate Metabolism. Methods Enzymol 1955; 17: 149–158.
  • Bilgehan H. Basic Microbiology and Immunology. İzmir: Faculties Bookstore Peace Publications; 1999. p.622.
  • Bilgin H. Antimicrobial activity of a bacteriocinogenic bacterium isolated from a fermented milk product. Master’s Thesis, Gaziosmanpaşa University, Tokat; 2008. p.55.
  • Bulut Ç. Isolation and characterization of lactic acid bacteria from cheese. Master’s Thesis, İzmir Institute of Technology, İzmir; 2003. p.112.
  • Chen J, Chen X, Dai J, Xie G, Yan L, Lu L, Chen J. Cloning, enhanced expression and characterization of an α-amylase gene from a wild strain in Bacillus subtilis WB800. Int J Biol Macromol 2015; 80: 200–207.
  • Chen Y, Yu L, Qiao N, Xiao Y, Tian F, Zhao J, Zhang H, Chen W, Zhai Q. Latilactobacillus curvatus: A candidate probiotic with excellent fermentation properties and health benefits. Foods 2020; 9: 1366.
  • De Angelis M, Gallo G, Corbo MR, McSweeney PLH, Faccia M, Giovine M, Gobbetti M. Phytase activity in sourdough lactic acid bacteria: purification and characterization of a phytase from Lactobacillus sanfrancisensis CB1. Int J Food Microbiol 2003; 87: 259–270.
  • Demain AL, Solomon NA. Manual of Industrial Microbiology & Biotechnology. Washington, DC: American Society for Microbiology; 1981. p.108.
  • Durak MZ, Fromm HI, Huck JR, Zadoks RN, Boor KJ. Development of molecular typing methods for Bacillus spp. and Paenibacillus spp. isolated from fluid milk products. J Food Sci 2006; 71.
  • Fincan SA, 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; 264: 118639.
  • Sudharhsan S, Senthilkumar S, Ranjith K. Physical and nutritional factors affecting the production of amylase from species of Bacillus isolated from spoiled food waste. Afr J Biotechnol 2007; 6: 430–435.
  • Bernfeld P. Amylases, α and β. In: Colowick SP, Kaplan NO, eds. Methods in Enzymology, Vol 1. New York, NY: Academic Press; 1955. p.149–158.
  • İspirli H. Tulum Peynirinden Laktik Asit Bakterilerinin (LAB) İzolasyonu, Moleküler Metotlarla TanımLanması ve Ekzopolisakkarit (EPS) Üretim Potansiyelinin Genetik Olarak Belirlenmesi. Master’s Thesis, Bayburt University, Bayburt; 2016. p.104.
  • Durak MZ, Fromm HI, Huck JR, Zadoks RN, Boor KJ. Development of molecular typing methods for Bacillus spp. and Paenibacillus spp. isolated from fluid milk products. J Food Sci 2006; 71.
  • Gänzle M, Ripari V. Composition and function of sourdough microbiota: From ecological theory to bread quality. Int J Food Microbiol 2016; 239: 19–25.
  • LaemmLi UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685.
  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the folin phenol reagent. J Biol Chem 1951; 193: 265–275.
  • Vishnu C, Seenayya G, Reddy G. Direct conversion of starch to L(+) lactic acid by amylase producing Lactobacillus amylophilus GV6. Bioprocess Eng 2000; 23: 155–158.
  • Orhan E. Enzyme activities of lactic bacteria and streptococci isolated from milk. Master’s Thesis, Gazi University Institute of Science and Technology, Ankara; 2013. p.118.
  • Songré-Ouattara LT, Mouquet-Rivier C, Icard-Vernière C, et al. Enzyme activities of lactic acid bacteria from a pearl millet fermented gruel (ben-saalga) of functional interest in nutrition. Int J Food Microbiol 2008; 128: 395–400.
  • Velikova P, Stoyanov A, Blagoeva G, Popova L, Petrov K, Gotcheva V, Petrova P. Starch utilization routes in lactic acid bacteria: New insight by gene expression assay. Starch/Stärke 2016; 68: 953–960.
  • Kanpiengjai A, Rieantrakoonchai W, Pratanaphon R, et al. High efficacy bioconversion of starch to lactic acid using an amylolytic lactic acid bacterium isolated from Thai indigenous fermented rice noodles. Food Sci Biotechnol 2014; 23: 1541–1550.
  • Unban K, Kanpiengjai A, Takata G, et al. Amylolytic enzymes acquired from L-lactic acid producing Enterococcus faecium K-1 and improvement of direct lactic acid production from cassava starch. Appl Biochem Biotechnol 2017; 183: 155–170.
  • Abiodun Onilude A, Solomon Ayinla G, Eluehike C. Properties of alpha amylase of Lactobacillus plantarum isolated from cassava waste samples. Biotechnol J Int 2017; 19: 1–14.
  • Sudan SK, Kumar N, Kaur I, Sahni G. Production, purification and characterization of raw starch hydrolyzing thermostable acidic α-amylase from hot springs, India. Int J Biol Macromol 2018; 117: 831–839.
  • Matpan Bekler F, Güven K, Gül Güven R. Purification and characterization of novel α-amylase from Anoxybacillus ayderensis FMB1. Biocatal Biotransform 2021;39:322–332.
  • Pan I. Exploration for thermostable β-amylase of a Bacillus sp. isolated from compost soil to degrade bacterial biofilm. Microbiol Spectr 2021; 9:e 0064721.
  • Zhao W, Zheng J, Wang YG, Zhou HB. A marked enhancement in production of amylase by Bacillus amyloliquefaciens in flask fermentation using statistical methods. J Cent South Univ Technol 2011; 18: 1054–1062.
  • Pandey A, Nigam P, Soccol CR, Soccol VT, Singh D, Mohan R. Advances in microbial amylases. J Biotechnol Appl Biochem 2000; 31: 135–152.
  • Pham VHT, Kim J, Shim J, Chang S, Chung W. Purification and characterization of strong simultaneous enzyme production of protease and α-amylase from an extremophile Bacillus sp. FW2 and its possibility in food waste degradation. Fermentation 2022; 8: 12.
  • Ragavan ML, Das N. In vitro studies on therapeutic potential of probiotic yeasts isolated from various sources. Curr Microbiol 2020; 77: 2821–2830.
  • Jo YM, Kim GY, Kim SA, Cheon SW, Kang CH, Han NS. Limosilactobacillus fermentum MG7011: An amylase and phytase producing starter for the preparation of rice-based probiotic beverages. Front Microbiol 2021; 12: 745952.
  • Stiles ME, Holzapfel WH. Lactic acid bacteria of foods and their current taxonomy. Int J Food Microbiol 1997; 36: 1–29.
  • Turpin W, Humblot C, Guyot JP. Genetic screening of functional properties of lactic acid bacteria in a fermented pearl millet slurry and in the metagenome of fermented starchy foods. Appl Environ Microbiol 2011; 77: 8722–8734.
  • Tallapragada P, Rayavarapu B, Purushothama RP, Naige RN, Pogakul VP. Screening of potential probiotic lactic acid bacteria and production of amylase and its partial purification. J Genet Eng Biotechnol 2018; 16: 357–362.
  • Giraud E, Gosselin L, Marin B, Parada JL, Raimbault M. Purification and characterization of an extracellular amylase from Lactobacillus plantarum strain A6. J Appl Bacteriol 1993; 75: 276–282.

Farklı fermente ürünlerden izole edilen laktik asit bakterilerinin alfa-amilaz aktivitesi: Latilactobacillus curvatus Y2-1B amilazının karakterizasyonu

Year 2025, Volume: 14 Issue: 2, 64 - 72, 27.06.2025
https://doi.org/10.46810/tdfd.1619709

Abstract

Bu çalışmada, doksan bir laktik asit bakterisi izolatı farklı fermente ürünlerden elde edilmiş ve α-amilaz üretme yetenekleri nişasta eklenmiş besiyeri kullanılarak kalitatif olarak incelenmiştir. İzole edilen suşlar arasından 75 LAB kalitatif olarak amilaz pozitif kabul edilmiş ve toplam 20 LAB'nin yüksek α-amilaz üretim yeteneğine sahip olduğu belirlenerek kantitatif α-amilaz enzim aktivitesi çalışmaları yapılmıştır. LAB'ler için kantitatif enzim aktivitesi sonuçları 1.283 U/mL- 13.670 U/mL aralığında bulunmuştur. Daha sonra, 3 LAB izolatı (P4-2B, Y2-1B, S1-2B) seçildi ve genotipik yöntemlerle tanımlanmıştır. Tanımlamadan sonra, enzim Latilactobacillus curvatusY2-1B izolatından kısmen saflaştırıldı ve pH, sıcaklık ve katyonların etkisini içeren aktivite analizleri belirlenmiştir. En düşük enzim aktivitesi pH 9'da 0.554 U/ml, en yüksek değer ise pH 6'da 0.694 U/ml olarak bulunmuştur (p<0.05). Öte yandan, saflaştırılan enzim SDS-PAGE'de yaklaşık 40kDa'lık bir bant oluştururken, amy genlerinin varlığı incelenmiş ve onaylanmıştır. Seçilen bu LAB izolatlarının α-amilaz enzim aktivitesinden dolayı endüstriyel biyoteknoloji ve mikrobiyal enzim endüstrisinde faydalı olabileceği değerlendirilmiştir.

Project Number

FYL-2021-11216

References

  • Abiodun Onilude A, Solomon Ayinla G, Eluehike C. Properties of Alpha-amylase of Lactobacillus plantarum Isolated from Cassava Waste Samples. Biotechnol J Int 2017; 19: 1–14.
  • Temel Y, Ayna A, Hamdi Shafeeq I, Ciftci M. In vitro effects of some antibiotics on glucose-6-phosphate dehydrogenase from rat (Rattus norvegicus) erythrocyte. Drug Chem Toxicol 2020; 43: 219–223.
  • Bayindir S, Ayna A, Temel Y, Ciftci M. The synthesis of new oxindoles as analogs of natural product 3,3″-bis(indolyl)oxindole and in vitro evaluation of the enzyme activity of G6PD and 6PGD. Turk J Chem 2018; 42: 332–345.
  • Bayindir S, Temel Y, Ayna A, Ciftci M. The synthesis of N‐benzoylindoles as inhibitors of rat erythrocyte glucose‐6‐phosphate dehydrogenase and 6‐phosphogluconate dehydrogenase. J Biochem Mol Toxicol 2018; 32: e22193.
  • Ataallahi E, Naderi-Manesh H, Roostaazad R, Yeganeh S. A simple 2-step purification process of α-amylase from Bacillus subtilis: Optimization by response surface methodology. Int J Biol Macromol 2021; 192: 64–71.
  • Axelsson LT. Lactic acid bacteria: classification and physiology. In: Salmina S, Wright AV, eds. Lactic Acid Bacteria. USA: Marcel Dekker Inc; 1993. p.1–63.
  • Bamigboye CO, Okonji RE, Oluremi IO, James V. Stain removing, juice-clarifying, and starch-liquefying potentials of amylase from Pleurotus tuberregium in submerged fermentation system. J Genet Eng Biotechnol 2022; 20: 23.
  • Bernfeld P. Enzymes Carbohydrate Metabolism. Methods Enzymol 1955; 17: 149–158.
  • Bilgehan H. Basic Microbiology and Immunology. İzmir: Faculties Bookstore Peace Publications; 1999. p.622.
  • Bilgin H. Antimicrobial activity of a bacteriocinogenic bacterium isolated from a fermented milk product. Master’s Thesis, Gaziosmanpaşa University, Tokat; 2008. p.55.
  • Bulut Ç. Isolation and characterization of lactic acid bacteria from cheese. Master’s Thesis, İzmir Institute of Technology, İzmir; 2003. p.112.
  • Chen J, Chen X, Dai J, Xie G, Yan L, Lu L, Chen J. Cloning, enhanced expression and characterization of an α-amylase gene from a wild strain in Bacillus subtilis WB800. Int J Biol Macromol 2015; 80: 200–207.
  • Chen Y, Yu L, Qiao N, Xiao Y, Tian F, Zhao J, Zhang H, Chen W, Zhai Q. Latilactobacillus curvatus: A candidate probiotic with excellent fermentation properties and health benefits. Foods 2020; 9: 1366.
  • De Angelis M, Gallo G, Corbo MR, McSweeney PLH, Faccia M, Giovine M, Gobbetti M. Phytase activity in sourdough lactic acid bacteria: purification and characterization of a phytase from Lactobacillus sanfrancisensis CB1. Int J Food Microbiol 2003; 87: 259–270.
  • Demain AL, Solomon NA. Manual of Industrial Microbiology & Biotechnology. Washington, DC: American Society for Microbiology; 1981. p.108.
  • Durak MZ, Fromm HI, Huck JR, Zadoks RN, Boor KJ. Development of molecular typing methods for Bacillus spp. and Paenibacillus spp. isolated from fluid milk products. J Food Sci 2006; 71.
  • Fincan SA, 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; 264: 118639.
  • Sudharhsan S, Senthilkumar S, Ranjith K. Physical and nutritional factors affecting the production of amylase from species of Bacillus isolated from spoiled food waste. Afr J Biotechnol 2007; 6: 430–435.
  • Bernfeld P. Amylases, α and β. In: Colowick SP, Kaplan NO, eds. Methods in Enzymology, Vol 1. New York, NY: Academic Press; 1955. p.149–158.
  • İspirli H. Tulum Peynirinden Laktik Asit Bakterilerinin (LAB) İzolasyonu, Moleküler Metotlarla TanımLanması ve Ekzopolisakkarit (EPS) Üretim Potansiyelinin Genetik Olarak Belirlenmesi. Master’s Thesis, Bayburt University, Bayburt; 2016. p.104.
  • Durak MZ, Fromm HI, Huck JR, Zadoks RN, Boor KJ. Development of molecular typing methods for Bacillus spp. and Paenibacillus spp. isolated from fluid milk products. J Food Sci 2006; 71.
  • Gänzle M, Ripari V. Composition and function of sourdough microbiota: From ecological theory to bread quality. Int J Food Microbiol 2016; 239: 19–25.
  • LaemmLi UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685.
  • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the folin phenol reagent. J Biol Chem 1951; 193: 265–275.
  • Vishnu C, Seenayya G, Reddy G. Direct conversion of starch to L(+) lactic acid by amylase producing Lactobacillus amylophilus GV6. Bioprocess Eng 2000; 23: 155–158.
  • Orhan E. Enzyme activities of lactic bacteria and streptococci isolated from milk. Master’s Thesis, Gazi University Institute of Science and Technology, Ankara; 2013. p.118.
  • Songré-Ouattara LT, Mouquet-Rivier C, Icard-Vernière C, et al. Enzyme activities of lactic acid bacteria from a pearl millet fermented gruel (ben-saalga) of functional interest in nutrition. Int J Food Microbiol 2008; 128: 395–400.
  • Velikova P, Stoyanov A, Blagoeva G, Popova L, Petrov K, Gotcheva V, Petrova P. Starch utilization routes in lactic acid bacteria: New insight by gene expression assay. Starch/Stärke 2016; 68: 953–960.
  • Kanpiengjai A, Rieantrakoonchai W, Pratanaphon R, et al. High efficacy bioconversion of starch to lactic acid using an amylolytic lactic acid bacterium isolated from Thai indigenous fermented rice noodles. Food Sci Biotechnol 2014; 23: 1541–1550.
  • Unban K, Kanpiengjai A, Takata G, et al. Amylolytic enzymes acquired from L-lactic acid producing Enterococcus faecium K-1 and improvement of direct lactic acid production from cassava starch. Appl Biochem Biotechnol 2017; 183: 155–170.
  • Abiodun Onilude A, Solomon Ayinla G, Eluehike C. Properties of alpha amylase of Lactobacillus plantarum isolated from cassava waste samples. Biotechnol J Int 2017; 19: 1–14.
  • Sudan SK, Kumar N, Kaur I, Sahni G. Production, purification and characterization of raw starch hydrolyzing thermostable acidic α-amylase from hot springs, India. Int J Biol Macromol 2018; 117: 831–839.
  • Matpan Bekler F, Güven K, Gül Güven R. Purification and characterization of novel α-amylase from Anoxybacillus ayderensis FMB1. Biocatal Biotransform 2021;39:322–332.
  • Pan I. Exploration for thermostable β-amylase of a Bacillus sp. isolated from compost soil to degrade bacterial biofilm. Microbiol Spectr 2021; 9:e 0064721.
  • Zhao W, Zheng J, Wang YG, Zhou HB. A marked enhancement in production of amylase by Bacillus amyloliquefaciens in flask fermentation using statistical methods. J Cent South Univ Technol 2011; 18: 1054–1062.
  • Pandey A, Nigam P, Soccol CR, Soccol VT, Singh D, Mohan R. Advances in microbial amylases. J Biotechnol Appl Biochem 2000; 31: 135–152.
  • Pham VHT, Kim J, Shim J, Chang S, Chung W. Purification and characterization of strong simultaneous enzyme production of protease and α-amylase from an extremophile Bacillus sp. FW2 and its possibility in food waste degradation. Fermentation 2022; 8: 12.
  • Ragavan ML, Das N. In vitro studies on therapeutic potential of probiotic yeasts isolated from various sources. Curr Microbiol 2020; 77: 2821–2830.
  • Jo YM, Kim GY, Kim SA, Cheon SW, Kang CH, Han NS. Limosilactobacillus fermentum MG7011: An amylase and phytase producing starter for the preparation of rice-based probiotic beverages. Front Microbiol 2021; 12: 745952.
  • Stiles ME, Holzapfel WH. Lactic acid bacteria of foods and their current taxonomy. Int J Food Microbiol 1997; 36: 1–29.
  • Turpin W, Humblot C, Guyot JP. Genetic screening of functional properties of lactic acid bacteria in a fermented pearl millet slurry and in the metagenome of fermented starchy foods. Appl Environ Microbiol 2011; 77: 8722–8734.
  • Tallapragada P, Rayavarapu B, Purushothama RP, Naige RN, Pogakul VP. Screening of potential probiotic lactic acid bacteria and production of amylase and its partial purification. J Genet Eng Biotechnol 2018; 16: 357–362.
  • Giraud E, Gosselin L, Marin B, Parada JL, Raimbault M. Purification and characterization of an extracellular amylase from Lactobacillus plantarum strain A6. J Appl Bacteriol 1993; 75: 276–282.
There are 43 citations in total.

Details

Primary Language English
Subjects Enzymes
Journal Section Articles
Authors

Şeyda Nur Turkay 0000-0002-6605-0989

Kevser Karaman 0000-0003-0729-6185

Hatice Bekiroğlu 0000-0003-3328-1550

Project Number FYL-2021-11216
Publication Date June 27, 2025
Submission Date January 14, 2025
Acceptance Date April 14, 2025
Published in Issue Year 2025 Volume: 14 Issue: 2

Cite

APA Turkay, Ş. N., Karaman, K., & Bekiroğlu, H. (2025). Alpha-amylase activity of lactic acid bacteria isolated from different fermented products: Characterization of Latilactobacillus curvatus Y2-1B amylase. Türk Doğa Ve Fen Dergisi, 14(2), 64-72. https://doi.org/10.46810/tdfd.1619709
AMA Turkay ŞN, Karaman K, Bekiroğlu H. Alpha-amylase activity of lactic acid bacteria isolated from different fermented products: Characterization of Latilactobacillus curvatus Y2-1B amylase. TJNS. June 2025;14(2):64-72. doi:10.46810/tdfd.1619709
Chicago Turkay, Şeyda Nur, Kevser Karaman, and Hatice Bekiroğlu. “Alpha-Amylase Activity of Lactic Acid Bacteria Isolated from Different Fermented Products: Characterization of Latilactobacillus Curvatus Y2-1B Amylase”. Türk Doğa Ve Fen Dergisi 14, no. 2 (June 2025): 64-72. https://doi.org/10.46810/tdfd.1619709.
EndNote Turkay ŞN, Karaman K, Bekiroğlu H (June 1, 2025) Alpha-amylase activity of lactic acid bacteria isolated from different fermented products: Characterization of Latilactobacillus curvatus Y2-1B amylase. Türk Doğa ve Fen Dergisi 14 2 64–72.
IEEE Ş. N. Turkay, K. Karaman, and H. Bekiroğlu, “Alpha-amylase activity of lactic acid bacteria isolated from different fermented products: Characterization of Latilactobacillus curvatus Y2-1B amylase”, TJNS, vol. 14, no. 2, pp. 64–72, 2025, doi: 10.46810/tdfd.1619709.
ISNAD Turkay, Şeyda Nur et al. “Alpha-Amylase Activity of Lactic Acid Bacteria Isolated from Different Fermented Products: Characterization of Latilactobacillus Curvatus Y2-1B Amylase”. Türk Doğa ve Fen Dergisi 14/2 (June 2025), 64-72. https://doi.org/10.46810/tdfd.1619709.
JAMA Turkay ŞN, Karaman K, Bekiroğlu H. Alpha-amylase activity of lactic acid bacteria isolated from different fermented products: Characterization of Latilactobacillus curvatus Y2-1B amylase. TJNS. 2025;14:64–72.
MLA Turkay, Şeyda Nur et al. “Alpha-Amylase Activity of Lactic Acid Bacteria Isolated from Different Fermented Products: Characterization of Latilactobacillus Curvatus Y2-1B Amylase”. Türk Doğa Ve Fen Dergisi, vol. 14, no. 2, 2025, pp. 64-72, doi:10.46810/tdfd.1619709.
Vancouver Turkay ŞN, Karaman K, Bekiroğlu H. Alpha-amylase activity of lactic acid bacteria isolated from different fermented products: Characterization of Latilactobacillus curvatus Y2-1B amylase. TJNS. 2025;14(2):64-72.

This work is licensed under the Creative Commons Attribution-Non-Commercial-Non-Derivable 4.0 International License.