Purification and partial characterization of a thiol proteinase from the thermophilic fungus Humicola lanuginosa.

Published

Journal Article

An extracellular thiol proteinase was produced by the growth of a thermophilic fungus, Humicola lanuginosa, on a medium containing 2% casein, and was purified to virtual homogeneity by affinity chromatography on organomercurial columns. The essential thiol group for activity was confirmed by the inhibition of the enzyme by p-chloromercuribenzoate and mercuric ions. The enzyme, purified 27-fold from the extracellular fluid, exhibited an Mr of 23700 on gel filtration and sedimentation equilibrium. The H. lanuginosa proteinase preferentially cleaves at the C-terminal end of hydrophobic amino acid residues. This proteinase differed from the plant enzyme papain in its interaction with three affinity matrices and its substrate specificity towards synthetic substrates. This enzyme represents a unique example of a thiol proteinase obtained from a fungal source.

Full Text

Duke Authors

Cited Authors

  • Shenolikar, S; Stevenson, KJ

Published Date

  • July 1, 1982

Published In

Volume / Issue

  • 205 / 1

Start / End Page

  • 147 - 152

PubMed ID

  • 6751320

Pubmed Central ID

  • 6751320

International Standard Serial Number (ISSN)

  • 0264-6021

Digital Object Identifier (DOI)

  • 10.1042/bj2050147

Language

  • eng

Conference Location

  • England