Antifungal Activity of Partially Purified Bacterial Chitinase Against <i>Alternaria alternata</i>

Dikbaş N., Uçar S., Tozlu E., Şenol Kotan M., Kotan R.

ERWERBS-OBSTBAU, cilt.65, sa.4, ss.761-766, 2023 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 65 Sayı: 4
  • Basım Tarihi: 2023
  • Doi Numarası: 10.1007/s10341-022-00716-4
  • Dergi Adı: ERWERBS-OBSTBAU
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Agricultural & Environmental Science Database, CAB Abstracts, Environment Index, Food Science & Technology Abstracts
  • Sayfa Sayıları: ss.761-766
  • Anahtar Kelimeler: Bacteria, L, coryniformis, Enzyme, Fungi, Biocontrol, BACILLUS-LICHENIFORMIS, PURIFICATION, SUBTILIS, ENZYME
  • Atatürk Üniversitesi Adresli: Evet

Özet

Alternative or complementary control methods need to be developed to reduce the use of hazardous chemicals in agriculture. Biological control of fungi by bacteria is an important alternative. The fungal cell wall consists of chitin, glucan, and glycoproteins. Therefore, bacteria producing hydrolytic enzymes such as chitinases are of great interest for degrading fungal cell wall components. Because of their safety, chitinases produced by lactic acid bacteria can be easily used in the agricultural industry for the control of chitin-rich phytopathogens. This study aimed to partially purify the chitinase enzyme from Lactobacillus coryniformis 3N11 and to determine its antifungal activity against Alternaria alternata ET57. The partially purified enzyme had an apparent molecular mass of 33 kDa. It indicated an optimum activity in pH 6 at 70 degrees C. The antifungal tests showed that it significantly inhibited the development of A. alternata ET57. The results suggest that the industrial use of chitinase enzyme purified from L. coryniformis 3N11 is advisable due to its wide pH range, high optimum temperature, and superior antifungal properties against A. alternata ET57.