Although sarcoplasmic proteins not directly impact muscle tenderness, their evaluation is useful to identify protein biomarkers related to meat quality parameters during post-mortem aging. Therefore, the aim of this research was to study the effect of aging on meat organoleptic properties and sarcoplasmic protein changes in 3 different horse muscles. 36 samples excised from longissimus lumborum (LL), semitendinosus (ST) and semimembranosus (SM) muscles of 12 Italian Heavy Draft Horse carcasses were analysed at 1, 3, 6, 9 and 14 days of aging. At each time, colour, texture profle analysis and changes of sarcoplasmic proteins with SDS-PAGE and Two-Dimensional Gel Electrophoresis (2DE) were estimated. ST muscle showed higher values of lightness and redness (P<0.001), while, LL muscle showed lower values (P<0.05) of hardness and chewiness parameters. During aging, a progressively decrease of hardness was observed in ST muscle reaching the lowest value at 14 days. Aging affected the intensities of several sarcoplasmic protein bands, particularly, band corresponding to glycogen phosphorylase b kinase decreased in intensity after 6 days of aging in LL muscle, and, after 14 days of aging, was almost disappeared. Additionally, LL muscle showed some polypeptides in the 28-20 kDa area starting from 6 days of aging. 2DE image analyses results showed a decrease of sarcoplasmic protein spots during aging reaching the lowest value in ST muscle at 14 days of aging. Proteins separation also revealed, at 14 days of aging, an increase of 2 spots of tropomyosin alpha and beta chains in the LL muscle. In addition, in ST spots ascribed to glycerol 3-phosphate dehydrogenase, superoxide dismutase and phosphoglucomutase-1 also revealed differences in abundance at 14 days. Data highlight that aging affect post-mortem biochemical processes with different intensities in each muscle and revealed potential protein biomarkers to monitor meat quality characteristics.
Proteome analysis of sarcoplasmic protein fraction associated with meat organoleptic characteristics
P. De Palo;A. Maggiolino;
2020-01-01
Abstract
Although sarcoplasmic proteins not directly impact muscle tenderness, their evaluation is useful to identify protein biomarkers related to meat quality parameters during post-mortem aging. Therefore, the aim of this research was to study the effect of aging on meat organoleptic properties and sarcoplasmic protein changes in 3 different horse muscles. 36 samples excised from longissimus lumborum (LL), semitendinosus (ST) and semimembranosus (SM) muscles of 12 Italian Heavy Draft Horse carcasses were analysed at 1, 3, 6, 9 and 14 days of aging. At each time, colour, texture profle analysis and changes of sarcoplasmic proteins with SDS-PAGE and Two-Dimensional Gel Electrophoresis (2DE) were estimated. ST muscle showed higher values of lightness and redness (P<0.001), while, LL muscle showed lower values (P<0.05) of hardness and chewiness parameters. During aging, a progressively decrease of hardness was observed in ST muscle reaching the lowest value at 14 days. Aging affected the intensities of several sarcoplasmic protein bands, particularly, band corresponding to glycogen phosphorylase b kinase decreased in intensity after 6 days of aging in LL muscle, and, after 14 days of aging, was almost disappeared. Additionally, LL muscle showed some polypeptides in the 28-20 kDa area starting from 6 days of aging. 2DE image analyses results showed a decrease of sarcoplasmic protein spots during aging reaching the lowest value in ST muscle at 14 days of aging. Proteins separation also revealed, at 14 days of aging, an increase of 2 spots of tropomyosin alpha and beta chains in the LL muscle. In addition, in ST spots ascribed to glycerol 3-phosphate dehydrogenase, superoxide dismutase and phosphoglucomutase-1 also revealed differences in abundance at 14 days. Data highlight that aging affect post-mortem biochemical processes with different intensities in each muscle and revealed potential protein biomarkers to monitor meat quality characteristics.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
