Research Paper | Published:

Hen Egg White Lysozyme Expressed in, and Secreted from, Aspergillus niger is Correctly Processed and Folded

Bio/Technology volume 8, pages 741745 (1990) | Download Citation

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Abstract

We transformed Aspergillus niger with the full length cDNA gene encoding hen eggwhite lysozyme (HEWL) and its secretion signal sequence. Lysozyme levels up to 12 mg/l were secreted when expression was controlled by the A. awamori glucoamylase (GAM) promoter and 1 mg/l when controlled by the A. nidulans glyceraldehyde-3-phosphate dehydrogenase (GPD) promoter. N-terminal sequence analysis of the recombinant protein indicated that the signal peptide was correctly processed by the A. niger secretory apparatus. The specific catalytic activity of the recombinant protein was identical to that of authentic hen lysozyme. The recombinant HEWL was examined by 2D 1H-NMR spectroscopy and shown to have a spectrum identical to that of authentic HEWL indicating that the protein was correctly folded.

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Author notes

    • David B. Archer

    Corresponding author.

Affiliations

  1. Agricultural and Food Research Council Institute of Food Research, Norwich Laboratory, Colney Lane, Norwich, NR4 7UA, U.K.

    • David B. Archer
    • , David J. Jeenes
    • , Donald A. MacKenzie
    • , Gale Brightwell
    •  & Nigel Lambert
  2. Dyson Perrins Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QY, U.K.

    • Gordon Lowe
    •  & Sheena E. Radford
  3. Inorganic Chemistry Laboraty, University of Oxford, South Parks Road, Oxford, OX1 3QR, U.K.

    • Sheena E. Radford
    •  & Christopher M. Dobson

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DOI

https://doi.org/10.1038/nbt0890-741