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A review of protein engineering for the food industry

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Abstract

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.

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  1. Institute of Food Research, Reading Laboratory, Earley Gate, Whiteknights Road, Reading, RG6 6BZ, UK

    P. W. Goodenough

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Goodenough, P.W. A review of protein engineering for the food industry. Mol Biotechnol 4, 151–166 (1995). https://doi.org/10.1007/BF02921609

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