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1.
Meat Sci ; 108: 109-14, 2015 Oct.
Article in English | MEDLINE | ID: mdl-26086346

ABSTRACT

Microwave spectroscopy has been applied in numerous non-food industry applications, and recently also in the food industry, for non-destructive measurements. In this study, a dry-cured ham model was designed and chemical analyses were performed for determining water activity, water content and salt content (sodium chloride) for all samples. These chemical parameters were also measured using microwave spectroscopy, with a rectangular microwave cavity resonator. Results indicate that microwave spectroscopy may be a promising technique for determination of water activity, salt content and water content in dry-cured ham using either reflected or transmitted signals.


Subject(s)
Food Analysis/methods , Food Quality , Meat Products/analysis , Meat/analysis , Microwaves , Animals , Desiccation , Muscle, Skeletal/chemistry , Salts/analysis , Spectrum Analysis , Swine , Water/analysis
2.
J Anim Sci ; 90(6): 2035-43, 2012 Jun.
Article in English | MEDLINE | ID: mdl-22178849

ABSTRACT

The aim of this study was to find potential biomarkers for meat tenderness in bovine Longissimus thoracis muscle and to compare results from isobaric Tag for Relative and Absolute Quantitation (iTRAQ) and 2-dimensional gel electrophoresis (2-DE) analysis. The experiment included 4 tender and 4 tough samples, based on shear force measurements at 7 d postmortem, from young Norwegian red (NRF) bulls, taken at 1 h postmortem. A number of the proteins which have previously been related to tenderness were found to change in abundance between tender and tough samples, both in iTRAQ (P < 0.1) and 2-DE analysis (P < 0.05). Furthermore, 3 proteins that have not previously been related to tenderness were found to change significantly in abundance between tender and tough meat samples in the present study. These include proteins related to control of flux through the tricarboxylate cycle [2-oxoglutarate dehydrogenase complex component E2 (OGDC-E2)], apoptosis (galectin-1) and regulatory role in the release of Ca(2+) from intracellular stores (annexin A6). Even though the overlap in significantly changing proteins was relatively low between iTRAQ and 2-DE analysis, certain proteins predicted to have the same function were found in both analyses and showed similar changes between the groups, such as structural proteins and proteins related to apoptosis and energy metabolism.


Subject(s)
Electrophoresis, Gel, Two-Dimensional/veterinary , Food Analysis/methods , Meat/standards , Muscle Proteins/chemistry , Muscle, Skeletal/chemistry , Animals , Biomarkers , Cattle/physiology , Food Technology , Male
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