Heterologous expression of a hyperthermophilic α-amylase in xanthan gum producing Xanthomonas campestris cells

Zoe Konsoula, Maria Liakopoulou-Kyriakides, Angelos Perysinakis, Panayiota Chira, Amalia Afendra, Constantin Drainas, Dimitrios A. Kyriakidis

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

A hyperthermophilic α-amylase encoding gene from Pyrococcus woesei was transferred and expressed in Xanthomonas campestris ATCC 13951. The heterologous α-amylase activity was detected in the intracellular fraction of X. campestris and presented similar thermostability and catalytic properties with the native P. woesei enzyme. The recombinant α-amylase was found to be stable at 90 °C for 4 h and within the same period it retained more than 50% of its initial activity at 110 °C. Furthermore, X. campestris transformants produced similar levels of recombinant α-amylase activity regardless of the carbon source present in the growth medium, whereas the native X. campestris α-amylase production was highly dependent on starch availability and it was suppressed in the presence of glucose or other reducing sugars. On the other hand, xanthan gum yield, which appeared to be similar for both wild type and recombinant X. campestris strains, was enhanced at higher starch or glucose concentrations. Evidence presented in this study supports that X. campestris is a promising cell factory for the co-production of recombinant hyperthermophilic α-amylase and xanthan gum.

Original languageEnglish
Pages (from-to)99-108
Number of pages10
JournalApplied Biochemistry and Biotechnology
Volume149
Issue number2
DOIs
Publication statusPublished - 1 May 2008

Keywords

  • α-amylase
  • Hyperthermophilicity
  • Xanthan gum
  • Xanthomonas campestris

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