Optimized medium improves expression and secretion of extremely thermostable bacterial xylanase, XynB, in Kluyveromyces lactis

J Microbiol Biotechnol. 2010 Nov;20(11):1471-80. doi: 10.4014/jmb.1005.05041.

Abstract

An extremely thermostable xylanase gene, xynB, from hyperthermophilic bacterium Thermotoga maritima MSB8 was successful expressed in Kluyveromyces lactis. Response surface methodology (RSM) was applied to optimize medium components for production of XynB secreted by the recombinant K. lactis. Secretion level (102 mg/L) and enzyme activity (49 U/ml) of XynB in the optimized medium (yeast extract, lactose, and urea; YLU) were much higher than those (56 mg/L, 16 U/ml) in original medium (yeast extract, lactose, and peptone; YLP). It was also observed that the secretory efficiency of mature XynB was improved by the YLU medium. mRNA levels of 13 characterized secretion-related genes between K. lactis cultured in YLP and YLU were detected using semi-quantitative RT-PCR method. It was found that unfolded protein response (UPR) related genes such as ero1, hac1, and kar2 were up-regulated in K. lactis cultured in YLU. Therefore, nutrient ingredient, especially nitrogen source had a significant influence on the XynB secretory efficiency in the host K. lactis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Culture Media / chemistry
  • Culture Media / metabolism
  • Endo-1,4-beta Xylanases / chemistry*
  • Endo-1,4-beta Xylanases / genetics
  • Endo-1,4-beta Xylanases / metabolism*
  • Enzyme Stability
  • Extracellular Space / chemistry
  • Extracellular Space / enzymology*
  • Extracellular Space / genetics
  • Gene Expression Regulation, Fungal
  • Gene Expression*
  • Kluyveromyces / genetics*
  • Kluyveromyces / metabolism
  • Protein Transport
  • Thermotoga maritima / enzymology*
  • Thermotoga maritima / genetics
  • beta-Glucosidase / chemistry*
  • beta-Glucosidase / genetics
  • beta-Glucosidase / metabolism*

Substances

  • Bacterial Proteins
  • Culture Media
  • beta-Glucosidase
  • Endo-1,4-beta Xylanases
  • XynB xylanase