In situ immobilization of β-galactosidase from Bacillus circulans in silica by sol-gel process: Application in prebiotic synthesis

Sindy Escobar, Andres Illanes, LORENA EVELYN WILSON SOTO, Claudia Bernal, Monica Mesa

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

The enzyme encapsulation is a very well-known stabilization pathway. However, there are some challenges in order to avoid the enzyme denaturation under encapsulation conditions. The β-galactosidase from Bacillus circulans was immobilized through sol-gel encapsulation route assisted by Triton X-100 surfactant and sugars. The effects of sugar presence in the immobilization process and the gelation time on the biocatalyst activity/stability were explained taking into account the characteristics of the formed silica matrix and the changes of the enzyme environment. The enzyme was effectively immobilized by this strategy, with high immobilization yield in terms of activity (29%) and expressed activity (47 IU/g). The immobilization through silica sol-gel in the presence of 1×10-3 M Triton X-100 and fructose conferred 28.4-fold higher stability to the enzyme compared with the soluble form. This is an advantage for its use in the synthesis of the galacto-oligosaccharides at 50oC. The total lactose conversion to galacto-oligosaccharides was 26%wt, which is comparable with that reported in the literature. The obtained biocatalyst is useful for the synthesis of galacto-oligosaccharides and its catalytic behavior is rationalized in this work.

Original languageEnglish
Pages (from-to)396-404
Number of pages9
JournalEngineering in Life Sciences
Volume16
Issue number4
DOIs
StatePublished - 1 May 2016
Externally publishedYes

Keywords

  • Enzyme encapsulation
  • Galacto-oligosaccharides
  • Lactose
  • Silica sol-gel process
  • Sugar protector

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