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Updated: Jul 6, 2026

Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation
Published on: January 16, 2019
Efficient bacterial expression of fusion proteins and their selective processing by a recombinant Kex-1 protease
Sabrina Pozzuolo1, Umberto Breme, Barbara Salis
1Bio-Ker S.R.L., Sardinia Scientific and Technological Park, Building 3, 09010 Pula, Cagliari, Italy.
Abstract:
A secreted, soluble variant of the Kex-1 endopeptidase from Kluyveromyces lactis has been produced and studied as a novel cleavage enzyme exhibiting high specificity for the Lys-Arg peptide. This highly selective, efficient enzyme is particularly adapted for use in manufacturing when a recombinant therapeutic protein, possessing its native N-terminus, has to be released in vitro from a bacterially-expressed fusion protein. In this paper, we describe the preparation of a Kex-1 variant using Saccharomyces cerevisiae and its application in the production of important therapeutic recombinant proteins such as human growth hormone, granulocyte colony-stimulating factor and interferon-alpha-2b.
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