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A review of protein engineering for the food industry
Author(s) -
GOODENOUGH P. W.
Publication year - 1995
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.1995.tb01364.x
Subject(s) - thermostability , protein folding , hydrogen bond , protein engineering , hydrophobic effect , food industry , relevance (law) , biochemical engineering , folding (dsp implementation) , protein stability , chemistry , nanotechnology , computer science , engineering , materials science , biochemistry , mechanical engineering , organic chemistry , food science , molecule , political science , law , enzyme
Summary In this review I briefly 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, disulphide bridges make to thermostability.