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.

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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105
09.12.2022 tarihinden bu yana
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enzyme PPPase presence activity determined optimum retained solution purified peptidase organic respectively increased solvents surfactants metallopeptidases showed compatible Triton xylene ethanol acetone whereas acetonitrile inactivation caused Characterization revealed neutral serine metallopeptidase purification efficiency chromatography affinity
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