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

Şeyda Nur Turkay; Kevser Karaman; Hatice Bekiroğlu

Makale detayları

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

Yazarlar:

Şeyda Nur Turkay | Kevser Karaman | Hatice Bekiroğlu

Yayıncı:

Bingol University

Ana Başlıklar:

Enzimler

Dergi:

Türk Doğa ve Fen Dergisi Vol.14 Issue 2, pp.64-72

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001352636

pISSN:

2149-6366

Anahtar kelimeler:

Özet:

 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 UmL- 13.670 UmL. 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 Uml at the pH 9 and 0.694 Uml at pH 6 as a highest value p0.05. 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.

 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 UmL- 13.670 UmL. 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 Uml at the pH 9 and 0.694 Uml at pH 6 as a highest value p0.05. 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.

 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 UmL- 13.670 UmL. 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 Uml at the pH 9 and 0.694 Uml at pH 6 as a highest value p0.05. 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.

 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 LABnin yüksek α-amilaz üretim yeteneğine sahip olduğu belirlenerek kantitatif α-amilaz enzim aktivitesi çalışmaları yapılmıştır. LABler için kantitatif enzim aktivitesi sonuçları 1.283 UmL- 13.670 UmL 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 9da 0.554 Uml, en yüksek değer ise pH 6da 0.694 Uml olarak bulunmuştur p0.05. Öte yandan, saflaştırılan enzim SDS-PAGEde yaklaşık 40kDalık 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.

Makale detayları

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

Yazarlar:

Şeyda Nur Turkay | Kevser Karaman | Hatice Bekiroğlu

Yayıncı:

Bingol University

Ana Başlıklar:

Enzimler

Dergi:

Türk Doğa ve Fen Dergisi Vol.14 Issue 2, pp.64-72

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001352636

pISSN:

2149-6366

Latilactobacillus curvatus

amylase

specific activity

thermostableLatilactobacillus curvatus

amilaz

spesifik aktivite

termostabil

Sayı

Makale detayları

Yazarlar: Şeyda Nur Turkay | Kevser Karaman | Hatice Bekiroğlu

Yayıncı: Bingol University

Ana Başlıklar: Enzimler

Dergi: Türk Doğa ve Fen Dergisi Vol.14 Issue 2, pp.64-72

Belge Tipi: Makale

Yayın Tarihi: 6/2025

Belge Dili: İngilizce

Document ID (Org No.): 2001352636

pISSN: 2149-6366

Sayı

Yazarlar:

Şeyda Nur Turkay | Kevser Karaman | Hatice Bekiroğlu

Yayıncı:

Bingol University

Ana Başlıklar:

Enzimler

Dergi:

Türk Doğa ve Fen Dergisi Vol.14 Issue 2, pp.64-72

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001352636

pISSN:

2149-6366