Biochemical identification of a lipoprotein with maltose-binding activity in the thermoacidophilic Gram-positive bacterium Alicyclobacillus acidocaldarius

Res Microbiol. Nov-Dec 1996;147(9):733-7. doi: 10.1016/s0923-2508(97)85120-0.

Abstract

Growth of the thermoacidophilic Gram-positive bacterium Alicyclobacillus acidocaldarius strain ATCC 27009 on maltose resulted in the increased production of a protein with apparent molecular mass of 40 kDa. By metabolic labelling with 14C-palmitic acid, the 40-kDa protein was identified as a lipoprotein. The protein exhibited maltose-binding activity at pH 3.5, as demonstrated by chromatography on cross-linked amylose. Partial amino acid sequence analysis revealed that the 40-kDa protein corresponds to the product of an open reading frame downstream from the amylase gene (amy) that displays similarity to enterobacterial maltose-binding proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus / classification
  • Bacillus / growth & development
  • Bacillus / physiology*
  • Carrier Proteins
  • Chromatography, Gel
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Lipoproteins / chemistry*
  • Lipoproteins / metabolism
  • Maltose / metabolism
  • Open Reading Frames

Substances

  • Carrier Proteins
  • Lipoproteins
  • Maltose