FOOD SCIENCE ›› 2010, Vol. 31 ›› Issue (3): 198-202.doi: 10.7506/spkx1002-6300-201003045

• Bioengineering • Previous Articles     Next Articles

Purification and Enzymatic Properties of Inulinase from Kluyveromyces marxianus

JIU Min WANG Lun-ji   

  1. Food and Bioengineering Department, Henan University of Science and Technology, Luoyang 471003, China
  • Received:2009-04-29 Revised:2009-08-24 Online:2010-02-01 Published:2010-12-29
  • Contact: JIU Min E-mail:jiumin0912@sohu.com

Abstract:

Crude extracellular inulinase from Kluyveromyces marxianus was purified through sequential steps of ultrafiltration, DEAE-cellulose anion exchange chromatography and SephadexG-100 gel filtration to obtain two components, designated as Exo I and Exo II inulinase. The molecular weight of Exo I inulinase was 85 kD. The optimal reaction pH and temperature of Exo I were 4.0 and 60 ℃, respectively. In addition, Mn2+and Mg2+ could improve the activity of Exo I inulinase; in contrast, Cu2+ and Fe2+ exhibited a strong inhibition effect on Exo I inulinase activity. Enzymatic hydrolysates of inulin by Exo I inulinase were fructose and a small amount of glucose.

Key words: Kluyveromyces marxianus, inulinase, purification, enzymatic property

CLC Number: