Dephytinization of food stuffs by phytase of Geobacillus sp TF16 immobilized in chitosan and calcium-alginate


Creative Commons License

Sirin Y., YILDIRIM AKATIN M. , ÇOLAK A. , SAĞLAM ERTUNGA N.

INTERNATIONAL JOURNAL OF FOOD PROPERTIES, vol.20, no.12, pp.2911-2922, 2017 (Journal Indexed in SCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 20 Issue: 12
  • Publication Date: 2017
  • Doi Number: 10.1080/10942912.2016.1261151
  • Title of Journal : INTERNATIONAL JOURNAL OF FOOD PROPERTIES
  • Page Numbers: pp.2911-2922
  • Keywords: Characterization, Dephytinization, Geobacillus, Immobilization, Phytase, Thermophilic, ASPERGILLUS-NIGER, PURIFICATION, DIGESTIBILITY, PHOSPHORUS, STABILIZATION, ALKALINE, ENZYMES, GROWTH, ACID, PH

Abstract

In this work, Geobacillus sp. TF16 phytase was separately immobilized in chitosan and Ca-alginate with the efficiency of 38% and 42%, respectively. These enzymes exhibited broad substrate specificity. Maximal relative phytase activity was measured at pH 5.0 and 95 degrees C and pH 3.0 and 75 degrees C for chitosan and Ca-alginate, respectively. The enzymes were highly stable in a wide pH and temperature range. Values of K-m and V-max were determined as 2.38 mM and 3401.36 U/mg protein for chitosan, and 7.5 mM and 5011.12 U/mg protein for Ca-alginate. The immobilized enzymes showed higher resistance to proteolysis. After 4 h incubation, hydrolysis capacities of chitosan- and Ca-alginate immobilized enzymes for soymilk phytate were calculated as 24% and 33%, respectively. The chitosan- and Ca-alginate immobilized phytases conserved its original activity after 8 and 6 cycles of reuse, respectively. The features of the enzymes were very attractive and they might be useful for some industrial applications.