Protein engineering to change thermal stability for food enzymes.
In this review we have briefly indicated how the present state of knowledge allows proteins to be mutated to increase or decrease stability. We have discussed experiments on both model proteins and those of relevance to the food industry, and show how hydrophobic forces are a major driving force for folding as well as having a major role in thermostability. We have also indicated the large contribution that hydrogen bonding, electrostatic interactions and, in a less well predicted way, disulphide bridges make to thermostability.
Goodenough
P W
PW
Department of Protein Engineering, A.F.R.C. Institute of Food Research, Reading Laboratory, Shinfield, U.K.
Jenkins
J A
JA
D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005502:Food; D005524:Food Technology / Q000379:methods*; D006358:Hot Temperature; D015202:Protein Engineering
D004798:Enzymes