Properties of Aspergillus niger Protease Isolated from Katsuobushi

Katsuobushi에서 분리한 Aspergillus niger protease의 효소학적성질

  • Kim, Kwan-Woo (Department of Food and Nutrition, Songwon Junior College) ;
  • Yun, Tai-Uk (Department of Food Science and Technology, Chung-ang University) ;
  • Kim, Jun-Pyong (Department of Food Science and Technology, Chung-ang University)
  • 김관우 (송원전문대 식품영양과) ;
  • 윤태욱 (중앙대학교 식품가공학과) ;
  • 김준평 (중앙대학교 식품가공학과)
  • Published : 1991.08.01


Protease was purified from Aspergillus niger propagated on katsuobushi. The optimal pH and temperature of the enzyme were 7.2 and $45^{\circ}C$, respectively. The enzyme was stable at $pH\;5{\sim}8$ and at below $40^{\circ}C$. Enzyme activity was promoted by $K^{-}\;and\;Fe^{2+}$, whereas it was inhibited by $Hg^{2},\;Zn^{2},\;Mn^{2}\;and\;Cd^{2}$. The acidic, basic and neutral amino acid compositions were found to be 22.63, 13.57 and 63.80%, respectively. The content of nonpolar, poler and sulfur-containing amino acids were 39.72, 20.03 and 9.53% respectively, and aspartic and glutamic acids were abundant. The molecular weight was 42,000 and isoelectric point was estimated pH 5.6.