Antimicrobial packaging to retard the growth of spoilage bacteria and to reduce the release of volatile metabolites in meat stored under vacuum at 1°C.

A nisin-EDTA solution was used for activation of the internal surface of plastic bags that were used to store beef chops at 1°C after vacuum packaging. The aim of the work was to evaluate the effect of the antimicrobial packaging on beef during storage. Volatile compounds and microbial populations were monitored after 0, 9, 20, 36, and 46 days of storage. The active packaging retarded the growth of lactic acid bacteria. Brochothrix thermosphacta was unable to grow for the whole storage time in treated samples, while the levels of Carnobacterium spp. in treated samples were below the detection limit for the first 9 days and reached loads below 5 Log CFU/cm(2) after 46 days. On the other hand, Enterobacteriaceae and Pseudomonas spp. were not affected by the use of the antimicrobial packaging and grew in all of the samples, with final populations of about 4 Log CFU/cm(2). Carnobacterium divergens was identified by PCR-denaturing gradient gel electrophoresis analysis of DNA extracted from beef after 36 days of storage. During beef storage, alcohols, aldehydes, ketones, and carboxylic acids were detected in the headspace of beef samples by solid-phase microextraction-gas chromatography-mass spectrometry analysis. The microbial metabolic activity was affected by the use of the antimicrobial film from the beginning up to 36 days with a maximum in the differences of volatile metabolites in samples analyzed at 20 days. The volatiles were also determined by electronic nose, allowing differentiation based on the time of storage and not on the type of packaging. The active packaging reduces the loads of spoilage microbial populations and the release of metabolites in the headspace of beef with a probable positive impact on meat quality.

Comparison of the frying performance of olive oil and palm superolein.

Deep-fat frying is an important method of food preparation in which foods are immersed in hot oil. Repeated use of frying oils is a common practice, and in the presence of atmospheric oxygen it produces various undesirable reactions in used oils. Stable frying oils usually require low linolenic acid (LnA < 3%), increased oleic acid (OA > 40%), and decreased linoleic acid (LA < 50%). The aim of this study was to establish the behavior of palm superolein (PSO) (OA 45%; LA 12.5%; LnA 0.2%) and olive oil (OO) during repeated, discontinuous deep frying of French fries. The behavior of the oils under controlled heating conditions was also studied by maintaining all of the process variables the same as those in deep frying, except that there was no food in the oil. The PSO selected to be tested in this study may represent an alternative to OO as a frying medium. Although PSO presented a faster increase in some oxidation indices, such as free fatty acid and total polar compounds, for other indicators, PSO showed better behavior than OO (less formation of C8:0 and lower peroxide value).

Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams.

The myofibrillar fraction of raw ham muscles and dry-cured hams with different ripening times was extracted in denaturing and reducing conditions and subjected to two-dimensional gel electrophoresis. The two-dimensional maps gave overall pictures of the already noted progressive disappearance of actin, tropomyosin and myosin light chains during ripening. In addition, two fragments from Myosin Heavy Chain proteolysis, marked as myosin chain fragments MCF1 and MCF2, were identified by immunodetection and matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF MS). Furthermore, a new form of actin on two-dimensional gel was identified by MALDI-TOF peptide mapping. In 12-month-old dry-cured ham, most myofibrillar proteins were completely hydrolyzed. At this stage of ripening, in fact, in some Parma and S. Daniele dry-cured ham samples, myosin heavy chain fragments and other unidentified neo-formed spots were found. Some of the sarcoplasmic proteins in water extracts from pork meat markedly decreased in amount or disappeared totally, during ripening. Surprisingly, two-dimensional gel electrophoresis maps of the water soluble protein fraction from dry-cured ham showed the presence of two spots identified as tropomyosin α- and ß-chain. This result suggests that some of the saline soluble myofibrillar proteins can disappear from this fraction because of salt solubilization and not due to complete enzyme action. Two-dimensional gel electrophoresis (2-DGE) has proved a powerful tool to evaluate the enzymatic susceptibility of meat proteins and the evolution of protein map fragmentation throughout ripening process as well as a means of obtaining a standard fingerprinting map characterizing the final product.