Efficient production from Aspergillus niger of a heterologous protein and an individual protein domain, heavy isotope-labelled, for structure-function analysis

J Biotechnol. 1996 Apr 30;46(2):85-93. doi: 10.1016/0168-1656(95)00179-4.

Abstract

Aspergillus niger has been used successfully to secrete proteins labelled with 13C and/or 15N to a specific activity of > 99% for high resolution NMR analysis. In the case of a heterologous protein, hen egg-white lysozyme, 15N single-labelled and 13C, 15N double-labelled forms were secreted at yields of 100-200 mg l-1 by optimising the type of carbon source used and the ratio of carbon to nitrogen. Another protein, the glucoamylase starch-binding domain from A. niger, was also produced as the 15N single-labelled form at 20-40 mg l-1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus niger / genetics
  • Aspergillus niger / metabolism*
  • Binding Sites
  • Carbon Isotopes
  • Glucan 1,4-alpha-Glucosidase / biosynthesis*
  • Glucan 1,4-alpha-Glucosidase / chemistry*
  • Glucan 1,4-alpha-Glucosidase / genetics
  • Isotope Labeling*
  • Magnetic Resonance Spectroscopy
  • Muramidase / biosynthesis*
  • Muramidase / chemistry*
  • Muramidase / genetics
  • Nitrogen Isotopes
  • Recombinant Proteins
  • Structure-Activity Relationship

Substances

  • Carbon Isotopes
  • Nitrogen Isotopes
  • Recombinant Proteins
  • Muramidase
  • Glucan 1,4-alpha-Glucosidase