Abstract
A fluorescent probe method using 8-anilino-l-naphthalene sulfonic acid (ANS) and all-trans-retinol (RET) has been used to study the effects of heat treatments on the hydrophobicity of meat proteins. The number of ANS binding sites per unit protein increased from 0.75 for unheated samples to 2.12 for meat proteins heated at 100° C for 30 min. The number of RET binding sites increased from 0.13 to 0.46 with the same heat treatment. This is discussed in terms of % increase in aromatic (182.7%) and aliphatic (253.5%) hydrophobicity for meat proteins heated at 100° C for 30 min. On the other hand, the assay was able to discriminate between samples of meat proteins receiving heat treatments with 100° C intervals (between 40 and 100° C).
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