Enhancement of immobilized enzyme activity by pretreatment of β-glucosidase with cellobiose and glucose

You Ree Jung, Hyun Yong Shin, Yoon Seok Song, Sung Bong Kim, Seung Wook Kim

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

In this study, β-glucosidase from Aspergillus niger was pretreated with cellobiose and glucose to prevent loss of enzyme activity, and pretreated β-glucosidase was immobilized on silica gel as a carrier by covalent binding. To enhance the activity of immobilized β-glucosidase, the effects of substrate concentration and reaction conditions, including temperature, time, and agitation speed, were investigated. The optimal concentrations of cellobiose and glucose, temperature, time, and agitation speed were determined to be 0.02. M, 40 °C, 20. min, and 130. rpm, respectively. The activity of immobilized β-glucosidase after pretreatment was increased to about 176% of that of non-pretreated β-glucosidase. In addition, the optimal pH and temperature of the non-pretreated and pretreated immobilized β-glucosidases were both pH 5.5 and 65 °C, respectively. Moreover, the immobilized β-glucosidases were used repeatedly 20 times, and the enzyme activities were maintained at levels higher than 80% of their initial activities.

Original languageEnglish
Pages (from-to)702-706
Number of pages5
JournalJournal of Industrial and Engineering Chemistry
Volume18
Issue number2
DOIs
Publication statusPublished - 2012 Mar 25

Keywords

  • Covalent binding
  • Enzyme pretreatment
  • Immobilization
  • Silica gel
  • β-Glucosidase

ASJC Scopus subject areas

  • Chemical Engineering(all)

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