Titre du document / Document title

Extracellular proteases produced by the Quorn® myco-protein fungus Fusarium graminearum in batch and chemostat culture

Auteur(s) / Author(s)

GRIFFEN A. M. ⁽¹⁾ ; WIEBE M. G. ⁽¹⁾ ; ROBSON G. D. ⁽¹⁾ ; TRINCI A. P. J. ⁽¹⁾ ;

Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)

⁽¹⁾ The School of Biological Sciences, 1.800 Stopford Building, University of Manchester, Manchester M13 9PT, ROYAUME-UNI

Résumé / Abstract

Fusarium graminearum was grown in batch and continuous (chemostat) culture on a glucose-mineral salts medium in the presence and absence of casein. In the absence of casein no protease activity was detected in the culture filtrate from either batch or chemostat culture. For batch cultures grown on medium containing casein, most of the proteolytic activity detected in the supernatant during exponential growth had an optimum at ca pH 5-0. However, as the cultures passed from late exponential into stationary phase, the pH profile of the protease activity broadened until most of it was in the alkaline pH region. For glucose-limited chemostat cultures grown on media containing casein, protease activity had a narrow pH optimum with maximum activity at pH 5-0. For all concentrations of casein examined, protease activity was greater in chemostat culture than in batch culture. Extracellular proteases from batch and chemostat cultures were purified by bacitracin-Sepharose affinity chromatography. At least seven proteins were purified from batch cultures but chemostat cultures contained only a single aspartic protease with a molecular mass of 40 kDa.

Revue / Journal Title

Microbiology   ISSN 1350-0872 

Source / Source

1997, vol. 143 (9), pp. 3007-3013 (29 ref.)

Langue / Language

Anglais

Editeur / Publisher

Society for General Microbiology, Reading, ROYAUME-UNI  (1994) (Revue)

Mots-clés anglais / English Keywords

Fusarium graminearum ; Acid proteinase ; Aspartic endopeptidases ; Extracellular ; Gene expression ; Batchwise ; Chemostat ; Fungi Imperfecti ; Fungi ; Thallophyta ; Peptidases ; Hydrolases ; Enzyme ; Bioreactor ;

Mots-clés français / French Keywords

Fusarium graminearum ; Acid proteinase ; Aspartic endopeptidases ; Extracellulaire ; Expression génique ; En discontinu ; Chémostat ; Fungi Imperfecti ; Fungi ; Thallophyta ; Peptidases ; Hydrolases ; Enzyme ; Bioréacteur ;

Mots-clés espagnols / Spanish Keywords

Fusarium graminearum ; Acid proteinase ; Aspartic endopeptidases ; Extracelular ; Expresión genética ; En discontinuo ; Quimostato ; Fungi Imperfecti ; Fungi ; Thallophyta ; Peptidases ; Hydrolases ; Enzima ; Biorreactor ;

Localisation / Location

INIST-CNRS, Cote INIST : 4410, 35400006924519.0190