Water Miscible Mono Alcohols' Effect on the Proteolytic Performance of Bacillus clausii Serine Alkaline Protease


DUMAN Y. , KAZAN D., Denizci A. A. , Erarslan A.

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, cilt.172, ss.469-486, 2014 (SCI İndekslerine Giren Dergi) identifier identifier identifier

  • Cilt numarası: 172 Konu: 1
  • Basım Tarihi: 2014
  • Doi Numarası: 10.1007/s12010-013-0525-3
  • Dergi Adı: APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
  • Sayfa Sayıları: ss.469-486

Özet

In this study, our investigations showed that the increasing concentrations of all examined mono alcohols caused a decrease in the V (m), k (cat) and k (cat)/K (m) values of Bacillus clausii GMBE 42 serine alkaline protease for casein hydrolysis. However, the K (m) value of the enzyme remained almost the same, which was an indicator of non-competitive inhibition. Whereas inhibition by methanol was partial non-competitive, inhibition by the rest of the alcohols tested was simple non-competitive. The inhibition constants (K (I)) were in the range of 1.32-3.10 M, and the order of the inhibitory effect was 1-propanol > 2-propanol > methanol > ethanol. The Delta G (not equal) and Delta G (not equal) (E -aEuro parts per thousand T) values of the enzyme increased at increasing concentrations of all alcohols examined, but the Delta G (not equal) (ES) value of the enzyme remained almost the same. The constant K (m) and Delta G (not equal) (ES) values in the presence and absence of mono alcohols indicated the existence of different binding sites for mono alcohols and casein on enzyme the molecule. The k (cat) of the enzyme decreased linearly by increasing log P and decreasing dielectric constant (D) values, but the Delta G (not equal) and Delta G (not equal) (E -aEuro parts per thousand T) values of the enzyme increased by increasing log P and decreasing D values of the reaction medium containing mono alcohols.