Premium
Dehalogenation of gaseous 1‐chlorobutane by dehydrated whole cells: Influence of the microenvironment of the halidohydrolase on the stability of the biocatalyst
Author(s) -
Marchand P.,
Lamare S.,
Legoy M.D.,
Goubet I.
Publication year - 2009
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.22286
Subject(s) - biocatalysis , chemistry , hydrolysis , intracellular , thermal stability , escherichia coli , extracellular , recombinant dna , denaturation (fissile materials) , catalysis , chemical engineering , biochemistry , organic chemistry , nuclear chemistry , reaction mechanism , engineering , gene
It was observed that a biocatalyst prepared from dehydrated whole cells of a recombinant Escherichia coli (initially suspended in borate buffer) was able to hydrolyze gaseous 1‐chlorobutane in a solid/gas reactor. Nevertheless, at 40°C and for a 0.7 water activity, it rapidly lost its activity. The explanation of this phenomenon was first investigated by observing the biocatalyst structure at the microscopic level and by studying the localization of the dehalogenase involved in catalysis (intracellular/ extracellular). The behavior of this biocatalyst was then compared with that of a preparation made from cells extracts. The reasons of the inactivation are discussed in terms of thermal denaturation and protective effect of buffer salts. Biotechnol. Bioeng. 2009;103: 687–695. © 2009 Wiley Periodicals, Inc.