volume 55, issue 1, P79-84 2007
DOI: 10.1002/jctb.280550113
View full text
|
Sign up to set email alerts
|
Share

Abstract: Abstract Thermal inactivation kinetics of native and glutaraldehyde cross‐linked forms of penicillin G acylase obtained from a mutant derivative of Escherichia coli ATCC 11105 were studied. Apparent activation energies for thermal inactivation of both native and cross‐linked forms of enzyme were calculated to be [57‐71 ± 8.46] and [67.11 ± 13.83] kcal mol−1 respectively. This slight increase in activation energy‐suggested that glutaraldehyde cross‐linking did not markedly protect against thermal inactivation.…

Expand abstract

Search citation statements

Order By: Relevance

Citation Types

0
2
0
1

Paper Sections

0
0
0
0
0

Publication Types

0
0
0
0

Relationship

0
0

Authors

Journals