Increasing importance of protein flexibility in designing biocatalytic processes
Enzymes require some flexibility for catalysis. Biotechnologists prefer stable enzymes but often this stabilization comes at the cost of reduced efficiency. Enzymes from thermophiles have low flexibility but poor catalytic rates. Enzymes from psychrophiles are less stable but show good catalytic rat...
Main Authors: | Joyeeta Mukherjee, Munishwar Nath Gupta |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
2015-06-01
|
Series: | Biotechnology Reports |
Subjects: | |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2215017X1500020X |
Similar Items
-
Dual bioimprinting of Thermomyces lanuginosus lipase for synthesis of biodiesel
by: Joyeeta Mukherjee, et al.
Published: (2016-06-01) -
Methods for affinity-based separations of enzymes and proteins /
by: Gupta, Munishwar Nath
Published: (2002) -
Cryptic genetic variation shapes the adaptive evolutionary potential of enzymes
by: Florian Baier, et al.
Published: (2019-02-01) -
Design of Artificial Enzymes Bearing Several Active Centers: New Trends, Opportunities and Problems
by: Diego Carballares, et al.
Published: (2022-05-01) -
Mechanistic Explanation of the Weak Carbonic Anhydrase’s Esterase Activity
by: Paolo Piazzetta, et al.
Published: (2017-06-01)