Partial purification and characterization of an extracellular metallopeptidase produced by bacillus amyloliquefaciens FE-K1

Erem, Fundagül | İnan, Mehmet | Karakaş Budak, Barçın | Certel, Muharrem

Article | 2020 |

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 Daha fazlası Daha az

Optimisation of bacillus amyloliquefaciens FE-K1 extracellular peptidase production by response surface methodology

Erem, Fundagül | İnan, Mehmet | Certel, Muharrem

Article | 2018 |

In this study, it was aimed to optimise the extracellular peptidase production of Bacillus amyloliquefaciens FE-K1, previously isolated from ropy wholemeal bread, by using response surface methodology (RSM) based on central composite design (CCD). The temperature (20-45°C), initial pH of the enzyme production medium (pH 5-9) and inoculation level (1-5%, v/v) were used as the factors for RSM, and the fermentation time was determined for each trial separately. Results showed that the optimum peptidase production occurred at 33.4°C, pH 6.62 and 2.3% inoculation. It was determined that the fermentation time was only 7h, the crude enzyme . . . had a peptidase activity of 49.17U/mL and a specific activity of 504.77U/mg under the optimised conditions Daha fazlası Daha az

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