Bacteriocins are ribosomal-synthesized antimicrobial peptides that inhibit the growing of pathogenic and/or deteriorating bacteria. The most studied bacteriocin-producing microorganisms are lactic acid bacteria (LAB), as they have great potential application in food biopreservation, since the majority have GRAS (Generally Recognized as Safe) status. The LAB-producing bacteriocins and/or bacteriocins produced by these bacteria have been widely studied, with the emphasis on those derived from milk and dairy products. On the other hand, isolates from meat and meat products are less studied. The objective of this review is to address the main characteristics, classification, and mechanism of action of bacteriocins and their use in food, to highlight studies on the isolation of LAB with bacteriocinogenic potential from meat and meat products and also to characterize, purify, and apply these bacteriocins in meat products. In summary, most of the microorganisms studied are Lactococcus, Enterococcus, Pediococcus, and Lactobacillus, which produce bacteriocins such as nisin, enterocin, pediocin, pentocin, and sakacin, many with the potential for use in food biopreservation.

This work aimed to evaluate the effects of particle size, solid/solvent ratio (w/v), and reaction time on hydrolytic and esterification activities of a lipase extract from wheat seeds. The higher hydrolytic activity was 5.9 U/g with a particle size of 425 microm, solid/solvent ratio of 30:60 (w/v), and reaction time of 15 h, with maximum hydrolytic activity of 14.47 U/g after 24 h of precipitation. For esterification activity the best result was 57.88 U/g with a particle size of 425 microm and solid/solvent ratio of 30:120 (w/v) for 5 h, with a maximum value after 10 h of precipitation reaching 208.20 U/g. The partial characterization showed that the optimal pH and temperature were found to be 5.5 and 32-37 degrees C, respectively. The extract stability at low temperatures was kept after 48 h of storage in terms of esterification activity. The hydrolytic activity was kept constant at -10 degrees C during 72 h and diminished considerably after 24 h at 4 degrees C.

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