A review of protein engineering for the food industry.
In this review I briefly describe the technique of protein engineering and indicate how the present state of knowledge allows proteins to be mutated to increase or decrease stability. I discuss 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. I also indicate the large contribution that hydrogen bonding, electrostatic interactions and, in a less well predicted way, disulfide bridges make to thermostability.
Goodenough
P W
PW
Institute of Food Research, Reading Laboratory, Earley Gate, UK.
D019747:Aldose-Ketose Isomerases; D001709:Biotechnology; D002238:Carbohydrate Epimerases / Q000737:chemistry / Q000235:genetics; D003545:Cysteine / Q000737:chemistry; D004563:Electrochemistry; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry / Q000235:genetics; D005524:Food Technology; D008958:Models, Molecular; D016296:Mutagenesis; D015202:Protein Engineering / Q000379:methods*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000235:genetics
D004798:Enzymes; D011506:Proteins; D002238:Carbohydrate Epimerases; D019747:Aldose-Ketose Isomerases; C023298:xylose isomerase; D003545:Cysteine