IMMUNOCHEMICAL QUANTIFICATION OF HEAT DENATURATION OF BOVINE MEAT SOLUBLE-PROTEINS

Citation
D. Levieux et al., IMMUNOCHEMICAL QUANTIFICATION OF HEAT DENATURATION OF BOVINE MEAT SOLUBLE-PROTEINS, Journal of food science, 60(4), 1995, pp. 678-684
Citations number
55
Categorie Soggetti
Food Science & Tenology
Journal title
ISSN journal
00221147
Volume
60
Issue
4
Year of publication
1995
Pages
678 - 684
Database
ISI
SICI code
0022-1147(1995)60:4<678:IQOHDO>2.0.ZU;2-2
Abstract
Immunoquantification of myoglobin, L-lactic dehydrogenases (LDH) M4 an d H4, albumin, transferrin and immunoglobulin G (TgG) was performed af ter heat treatment of crude soluble sarcoplasmic protein extract over a range of 54-70 degrees C for 30-780 min. Heat denaturation occurred in the following order: transferrin > IgG > LDH M4 > LDH H4 = myoglobi n > albumin and could be described by first order reaction kinetics. T he very low coefficient of variation (2-4%) of the single radial immun odiffusion technique resulted in a very weak calculated error (+/-0.1- 0.2 degrees C) on temperature determination Monitoring the concentrati on of LDH M4 appears appropriate for determining the minimum heating a chieved in long-time, low-temperature cooking and albumin or myoglobin could be monitored for meat cooked at 69 degrees C without holding ti me.