Partial Purification and Characterization of Thermostable, Alkaline and Chelator- resistant Protease from a Newly Isolated Bacillus sp. CY7 and its potential applications  in various industries

Nihan ARABACI; Yasemin CAF; Yelis MAAŞOĞLU; Burhan ARIKAN

Makale detayları

Partial Purification and Characterization of Thermostable, Alkaline and Chelator- resistant Protease from a Newly Isolated Bacillus sp. CY7 and its potential applications in various industries

Yazarlar:

Nihan ARABACI | Yasemin CAF | Yelis MAAŞOĞLU | Burhan ARIKAN

Yayıncı:

Nobel Bilim ve Araştırma Merkezi Limited

Dergi:

Journal of Applied Biological Sciences 2013 Vol.7 Issue 2, pp.14-19

Belge Tipi:

Makale

Yayın Tarihi:

6/2013

Belge Dili:

Türkçe

Document ID (Org No.):

2000831420

Sıklık:

Üç Yıllık

eISSN:

2146-0108

Özet:

 

A thermophile alkaline protease producing Bacillus sp. strains isolated from soil samples. Enzyme synthesis occurred at temperatures between 20ºC and 60ºC with an optimum of 55°C and between the pH range of 6.0-13.0 with an optimum pH of 10.0 on skimmilk agar plates. Analyses of molecular mass of the partially purified enzyme was carried out by SDS-PAGE which revealed two bands as 112 and 97 kDa. The enzyme was active in a broad temperature range between 30ºC and 100ºC, with an optimum at 70ºC, and maximum activity was at pH 11.0. The enzyme also presented the alkaline-stable properties with a remaining activity around 94%, at pH 6.0-13.0 for 24 h, at 55°C. The enzyme activity was highly stable between 30-100°C with a remaining activity 91%, after pre-incubation for 1 h. Enzyme was exposured to various NaCl concentrations (3-30%), and the highest residual activity was determined in the presence of 3% NaCl (87%). While after being exposed with β-mercaptoethanol (1%), PMSF (3mM), Tween20 (0.1%), Tween80 (0.1%), SDS (1%), TritonX100 (1%), H2O2 (1%), MnCl2 (5mM), CaCl2 (5mM), BaCl2 (5mM), MgCl (5mM), FeCl2 (5mM) and EDTA (5mM), the enzyme exhibited the following activities 105%, 101%, 107%, 119%, 72%, 99%, 98%, 98%, 99%, 98%, 97%, 97%, 96% and 99%, respectively. According to these results, CY7 protease shows thermostable, high alkaline, alkali-stable and chelator resistant properties. Owing to its mentioned properties this protease is an ideal choice for application in detergent formulations, leather and textile industries.

Makale detayları

Partial Purification and Characterization of Thermostable, Alkaline and Chelator- resistant Protease from a Newly Isolated Bacillus sp. CY7 and its potential applications in various industries

Yazarlar: Nihan ARABACI | Yasemin CAF | Yelis MAAŞOĞLU | Burhan ARIKAN

Yayıncı: Nobel Bilim ve Araştırma Merkezi Limited

Dergi: Journal of Applied Biological Sciences 2013 Vol.7 Issue 2, pp.14-19

Belge Tipi: Makale

Yayın Tarihi: 6/2013

Belge Dili: Türkçe

Document ID (Org No.): 2000831420

Sıklık: Üç Yıllık

eISSN: 2146-0108

Sayı

Yazarlar:

Nihan ARABACI | Yasemin CAF | Yelis MAAŞOĞLU | Burhan ARIKAN

Yayıncı:

Nobel Bilim ve Araştırma Merkezi Limited

Dergi:

Journal of Applied Biological Sciences 2013 Vol.7 Issue 2, pp.14-19

Belge Tipi:

Makale

Yayın Tarihi:

6/2013

Belge Dili:

Türkçe

Document ID (Org No.):

2000831420

Sıklık:

Üç Yıllık

eISSN:

2146-0108