Recombinant production and characterization of Aspergillus niger prolyl endopeptidase enzyme for gluten-free food production    
Yazarlar (4)
Belma Şenol
Sivas Cumhuriyet Üniversitesi, Türkiye
Özlem Kaplan
Alanya Alaaddin Keykubat Üniversitesi, Türkiye
Rizvan İmamoğlu
Bartın Üniversitesi, Türkiye
Prof. Dr. İsa GÖKÇE Tokat Gaziosmanpaşa Üniversitesi, Türkiye
Makale Türü Açık Erişim Özgün Makale
Makale Alt Türü Ulusal alan endekslerinde (TR Dizin, ULAKBİM) yayınlanan tam makale
Dergi Adı International Journal of Agriculture, Environment and Food Sciences
Dergi ISSN 2602-246X
Dergi Tarandığı Indeksler TR DİZİN
Makale Dili İngilizce
Basım Tarihi 08-2021
Cilt No 5
Sayı 3
Sayfalar 287 / 293
DOI Numarası 10.31015/jaefs.2021.3.5
Makale Linki http://dx.doi.org/10.31015/jaefs.2021.3.5
Özet
Gluten is a protein group found in wheat, barley, rye, and oats, known as cereals. When this vegetable protein is introduced into the body, celiac disease can occurs. The use of bacterial and fungal oligopeptidase to ensure the cleavage of gluten into non-toxic fragments are considered a promising alternative for celiac disease. In this study, the Aspergillus niger Prolyl EndoPeptidase (AN-PEP) enzyme was cloned into pET22b vector and recombinantly produced in BL21 (DE3) pLysE cells. PEP enzyme expressed as inclusion body and was recovered by refolding. And N-terminal His-tagged recombinant protein was purified by nickel affinity chromatography. 280 mg AN-PEP enzyme from 1L bacterial culture was purified at very high yield, and this protein was 90% purity. As a result; It has been determined that the recombinantly produced PEP enzyme can digest gluten. This study shows that recombinantly produced AN-PEP (rAN-PEP) has great potential to use in the production processes of gluten-free foods.
Anahtar Kelimeler
Gluten | Celiac disease | Aspergillus niger