Premium
ON THE NATURE OF THE CHEMICAL AND PHYSICAL BONDS WHICH CONTRIBUTE TO SOME STRUCTURAL PROPERTIES OF PROTEIN FOODS: A HYPOTHESIS
Author(s) -
BUTTKUS H.
Publication year - 1974
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1974.tb02930.x
Subject(s) - chemistry , hydrogen bond , myosin , guanidine , sodium borohydride , hydrophobic effect , salt (chemistry) , disulfide bond , non covalent interactions , amino acid , peptide , denaturation (fissile materials) , molecule , biophysics , biochemistry , organic chemistry , catalysis , nuclear chemistry , biology
Extractability of the contractile proteins of muscle with salt solutions decreases during freezer storage or on heating. Studies on the insolubilized proteins with dissociating‐reducing solutions containing guanidine HCl (GuHCl) and mercaptoethanol or sodium borohydride (NaBH 4 ) have previously suggested that the mechanisms of myosin aggregation in solution involve noncovalent interactions of hydrophobic and hydrogen bonds as well as the formation of disulfide (S‐S) bonds between peptide chains of different molecules. Further evidence is now presented which implies that these types of denaturation mechanisms are of a more general nature and are also responsible in the hardening, fuming or gelling of the protein structures of egg white, kamaboko and meats from fish and mammals during cooking. Methods are described by which foods whose structures are dependent upon these types of bonds can be dissolved nonhydrolytically, i.e., without excessive breaking of peptide chains and the destruction or racemization of amino acids which occur during acid or alkaline treatment at elevated temperatures.