Performance of β-galactosidase pretreated with lactose to prevent activity loss during the enzyme immobilisation process

Yoon Seok Song, Jong Ho Lee, Seong Woo Kang, Seung Wook Kim

Research output: Contribution to journalArticlepeer-review

35 Citations (Scopus)

Abstract

In this study, Kluyveromyces lactis β-galactosidase was pretreated with lactose to prevent loss of activity during the immobilisation process, and glutaraldehyde was used as a linker to immobilise β-galactosidase on the surface of a silica gel. The pretreatment of β-galactosidase strongly improved its activity after immobilisation. Specifically, the activity of pretreated immobilised β-galactosidase was 2.6 times greater than that of non-pretreated immobilised β-galactosidase. The optimal temperature, pH and ionic strength of buffer for pretreated immobilised β-galactosidase were 37 °C, pH 7.5 and 20 mM potassium phosphate buffer, respectively. These values were shifted by 5 °C and pH by 0.5 when compared to the soluble β-galactosidase. Moreover, the pretreated immobilised β-galactosidase showed a better reusability than did non-pretreated immobilised β-galactosidase, with 63.9% of its original activity being retained after 10 reuses.

Original languageEnglish
Pages (from-to)1-5
Number of pages5
JournalFood Chemistry
Volume123
Issue number1
DOIs
Publication statusPublished - 2010 Nov 1

Keywords

  • Immobilisation
  • Lactose
  • Pretreatment
  • Silica gel
  • β-Galactosidase

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

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