Purification and characterization of thermoactive serratiopeptidase from Serratia marcescens AD-W2
| Autor: | Asha Chaubey, Md. Mehedi Hossain, Diksha Koul, Jasmine Kour Khosla, Mohd Jamal Dar, Devtulya Chander |
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| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
lcsh:Biotechnology lcsh:QR1-502 Biophysics 01 natural sciences Applied Microbiology and Biotechnology lcsh:Microbiology Metalloprotease 03 medical and health sciences Serratiopeptidase lcsh:TP248.13-248.65 Casein Serratia marcescens Histidine 030304 developmental biology 0303 health sciences Chromatography biology Molecular mass Chemistry Proteolytic enzymes Correction biology.organism_classification Serralysin Original Article Specific activity Homology modelling 010606 plant biology & botany |
| Zdroj: | AMB Express AMB Express, Vol 11, Iss 1, Pp 1-10 (2021) |
| ISSN: | 2191-0855 |
| Popis: | Serratiopeptidase is a proteolytic enzyme extensively used as an anti-inflammatory and analgesic drug. Present work reports a thermoactive serratiopeptidase from Serratia marcescens AD-W2, a soil isolate from the North-Western Himalayan region of India. The extracellular metalloprotease has been purified by a simple two-step procedure resulting in a specific activity of 20,492 Units/mg protein with 5.28-fold purification. The molecular mass of the metalloprotease, as determined by SDS-PAGE was ~ 51 kDa. The purified serratiopeptidase presented optimum activity at pH 9.0, temperature 50 °C and stability in wide pH and temperature range. Critical temperature of 50 °C confirmed the thermoactivity of the purified serratiopeptidase. The kinetic studies of the purified serratiopeptidase revealed Vmax and Km of 57,256 Units/mL and 1.57 mg/mL, respectively, for casein. The purified serratiopeptidase from S. marcescens AD-W2 was found to be 100% identical to serralysin from Serratia marcescens ATCC 21074/E-15. The catalytic domain comprising of Zn coordinated with three histidine residues (His192, His196, His202), along with glutamate (Glu193) and tyrosine (Tyr232) residues, further confirmed that the purified protein is identical to serralysin. |
| Databáze: | OpenAIRE |
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