Partial purification and characterization of an extracellular metallopeptidase produced by bacillus amyloliquefaciens FE-K1
The aim of this study was to purify and characterize the peptidase of Bacillus amyloliquefaciens (Fukumoto) (strain FE-K1) isolated from ropey bread. Peptidases were purified from crude enzyme solution by affinity chromatography with an efficiency of 25 % and a purification coefficient of 1.53. The optimum pH of partially purified peptidase (PPPase) solution was determined as 7.5 and the peptidases retained approximately 90 % of their initial activity in the pH range 7.0-8.5 following incubation at 37°C for 2 h. The optimum temperature for the PPPase was 60°C. The approximate molecular weight of the PPPase was determined as 36 kDa. Inactivation of the PPPase in the presence of O-FEN and EDTA showed them to be metallopeptidases and 5 mM of K+1 and 5 mM of Mn+2 ions increased the enzyme activity by 4 % and 6.15 %, respectively. The presence of Hg+2, Fe+3 and SDS (0.1-1.0 % w/v) caused inactivation whereas the enzyme retained most of its activity in the presence of 0.1-1.0 % (v/v) Triton X-100, Tween 20 and Tween 80 and 1-20 % (v/v) xylene, ethanol, acetone and acetonitrile. Characterization of the PPPase revealed the enzyme as a neutral serine metallopeptidase compatible with some organic solvents and surfactants.
| Yazar |
Erem, Fundagül İnan, Mehmet Karakaş Budak, Barçın Certel, Muharrem |
| Yayın Türü | Article |
| Tek Biçim Adres | https://hdl.handle.net/20.500.12628/9418 |
| Konu Başlıkları |
Bacillus amyloliquefaciens
metallopeptidase ropy bread purification |
| Koleksiyonlar |
Fakülteler Mühendislik Fakültesi Gıda Mühendisliği Bölümü Makale Koleksiyonu (Gıda Mühendisliği Bölümü) Araştırma Çıktıları | WoS | Scopus | TR-Dizin | PubMed | SOBİAD TR-Dizin İndeksli Yayınlar Koleksiyonu Araştırma Çıktıları | WoS | Scopus | TR-Dizin | PubMed | SOBİAD WoS İndeksli Yayınlar Koleksiyonu |
| Dergi Cilt Bilgisi | 21 |
| Dergi Sayısı | 1 |
| Sayfalar | 47 - 61 |
| Yayın Yılı | 2020 |
| Eser Adı [dc.title] | Partial purification and characterization of an extracellular metallopeptidase produced by bacillus amyloliquefaciens FE-K1 |
| Yazar [dc.contributor.author] | Erem, Fundagül |
| Yazar [dc.contributor.author] | İnan, Mehmet |
| Yazar [dc.contributor.author] | Karakaş Budak, Barçın |
| Yazar [dc.contributor.author] | Certel, Muharrem |
| Yayın Yılı [dc.date.issued] | 2020 |
| Yayın Türü [dc.type] | article |
| Özet [dc.description.abstract] | The aim of this study was to purify and characterize the peptidase of Bacillus amyloliquefaciens (Fukumoto) (strain FE-K1) isolated from ropey bread. Peptidases were purified from crude enzyme solution by affinity chromatography with an efficiency of 25 % and a purification coefficient of 1.53. The optimum pH of partially purified peptidase (PPPase) solution was determined as 7.5 and the peptidases retained approximately 90 % of their initial activity in the pH range 7.0-8.5 following incubation at 37°C for 2 h. The optimum temperature for the PPPase was 60°C. The approximate molecular weight of the PPPase was determined as 36 kDa. Inactivation of the PPPase in the presence of O-FEN and EDTA showed them to be metallopeptidases and 5 mM of K+1 and 5 mM of Mn+2 ions increased the enzyme activity by 4 % and 6.15 %, respectively. The presence of Hg+2, Fe+3 and SDS (0.1-1.0 % w/v) caused inactivation whereas the enzyme retained most of its activity in the presence of 0.1-1.0 % (v/v) Triton X-100, Tween 20 and Tween 80 and 1-20 % (v/v) xylene, ethanol, acetone and acetonitrile. Characterization of the PPPase revealed the enzyme as a neutral serine metallopeptidase compatible with some organic solvents and surfactants. |
| Kayıt Giriş Tarihi [dc.date.accessioned] | 2021-03-26 |
| Açık Erişim Tarihi [dc.date.available] | 2021-03-26 |
| Yayın Dili [dc.language.iso] | eng |
| Konu Başlıkları [dc.subject] | Bacillus amyloliquefaciens |
| Konu Başlıkları [dc.subject] | metallopeptidase |
| Konu Başlıkları [dc.subject] | ropy bread |
| Konu Başlıkları [dc.subject] | purification |
| Künye [dc.identifier.citation] | Erem, F., Inan, M., Karakas Budak, B. ve Certel, M. (2020). Partial purification and characterization of an extracellular metallopeptidase produced by bacillus amyloliquefaciens fe-k1. Trakya University Journal of Natural Sciences, 21(1), 47-61. doi:10.23902/trkjnat.647525 |
| Haklar [dc.rights] | info:eu-repo/semantics/openAccess |
| İlk Sayfa Sayısı [dc.identifier.startpage] | 47 |
| Son Sayfa Sayısı [dc.identifier.endpage] | 61 |
| Dergi Sayısı [dc.identifier.issue] | 1 |
| Dergi Cilt Bilgisi [dc.identifier.volume] | 21 |
| Tek Biçim Adres [dc.identifier.uri] | https://hdl.handle.net/20.500.12628/9418 |
| Tek Biçim Adres [dc.identifier.uri] | https://doi.org/10.23902/trkjnat.647525 |
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