A review of protein engineering for the food industry.

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.

journal_name

Mol Biotechnol

journal_title

Molecular biotechnology

authors

Goodenough PW

doi

10.1007/BF02921609

subject

Has Abstract

pub_date

1995-10-01 00:00:00

pages

151-66

issue

2

eissn

1073-6085

issn

1559-0305

journal_volume

4

pub_type

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