Irreversible lysozyme inactivation and aggregation induced by stirring : kinetic study and aggregates characterisation

Stirring strongly enhanced irreversible inactivation and aggregation of lysozyme being studied as a model enzyme. From 0 to 740 rpm (equivalent to impeller tip speeds from 0 to 0.77 m s^sup -1^), the inactivation kinetic constant was proportional to the power imparted by the impeller. Collisions bet...

Full description

Saved in:
Bibliographic Details
Published inBiotechnology letters Vol. 22; no. 4; pp. 277 - 283
Main Authors COLOMBIE, S, GAUNAND, A, RINAUDO, M, LINDET, B
Format Journal Article
LanguageEnglish
Published Dordrecht Springer 01.02.2000
Springer Nature B.V
Subjects
Aggregates
Biological and medical sciences
Biotechnology
Enzyme engineering
Enzymes
Fundamental and applied biological sciences. Psychology
Impellers
Inactivation
Kinetics
Methods. Procedures. Technologies
Miscellaneous
Aggregation
Bioreactor
Enzyme
Glycosidases
Hydrolases
Kinetics
Inactivation
O-Glycosidases
Lysozyme
Stirred tank reactor
Online AccessGet full text

Cover

More Information
Summary:Stirring strongly enhanced irreversible inactivation and aggregation of lysozyme being studied as a model enzyme. From 0 to 740 rpm (equivalent to impeller tip speeds from 0 to 0.77 m s^sup -1^), the inactivation kinetic constant was proportional to the power imparted by the impeller. Collisions between inactive and native molecules induced inactivation of the latter and led to lysozyme aggregation. These fractal aggregates of lysozyme were made of monomers, dimers and trimers.[PUBLICATION ABSTRACT]
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0141-5492
1573-6776
DOI:10.1023/A:1005655005780