Catheptic Enzymes and Meat Tenderization (original) (raw)
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Cathepsin involvement in muscle proteolysis in meat-type bulls
Czech Journal of Animal Science, 2005
ABSTRACT: Measurements were done of some lysosomal proteolytic enzyme activities involved in skeletal muscle proteolysis of the masculus longissimus lumborum et thoracis muscle (MLLT) of bulls. Samples from the same region between the 11th and 13th vertebra were taken after slaughter from Limousin (n= 10), Hereford (n= 10), Charolais (n= 10), Angus (n= 11) and Simmental (n= 11) bulls about 15 months old fed complete diet ad libitum. The activity of cathepsin D was determined as pepstatin (cathepsin D inhibitor) ...
Assay of Cathepsin D activity in fresh pork muscle and dry-cured ham
Meat Science, 1991
A BS TRA C T Different assays of cathepsin D activity in both porcine muscle and dry-cured ham extracts have been tested in order to find the best conditions for a reliable detection of cathepsin D in dry-cured meat products. The enzyme was effectively extracted with 0"2% (v/v) of Triton X-IO0. Nucleases if present were not observed to interfere with the assays. The best conditions for a reliable detection of cathepsin D in dry-cured ham were found to be the incubation of the enzyme extract for 1 h at 45°C in a reaction mixture containing 0"60% (w/v) of haemoglobin in 0"2 M sodium citrate buffer, pH = 3"7.
Problems associated with the assay of cathepsin D in meat and meat products
Food Chemistry, 1991
Cathepsin D is usually assayed by following the release of the trichloroacetic (TCA)-soluble peptides from denatured haemoglobin at 280nm, but some artefacts may appear giving false results. Cathepsin D activity has therefore been assayed under different conditions in muscle, liver and dry-cured ham extracts. Substantial errors (around 50-56 %) become evident when using the classical standard assay. The assay of cathepsin D activity in muscle extracts should include the use of a blank containing a specific inhibitor such as isovaler ylpepstatin.
Activity of cathepsins during beef aging related to mutations in the myostatin gene
Journal of The Science of Food and Agriculture, 2007
Double-muscled syndrome in cattle improves meat tenderness. However, the nature of the proteolytic processes associated with this phenomenon remains unknown. The aim of this study was to monitor changes in the activity of cathepsins (B, B + L, D and H) during meat aging and their gradual release from lysosomes to the cytosol in the longissimus muscle of yearling bulls of two breeds from northern Spain (Asturiana de los Valles and Asturiana de la Montaña) showing three genotypes for muscular hypertrophy (mh/mh, mh/+ and + / +). The data showed that the pattern of cathepsin activity during meat aging paralleled variations in tenderness in the different genotypes studied. Maximal cathepsin D activity and minimal cathepsin H activity were recorded during meat aging times ranging from 3 to 21 days. The activities of cathepsins B and B + L were lower than that of cathepsin D at the established time points (3, 7, 14 and 21 days post-slaughter). The role of these enzymes in the activation of cathepsin D is discussed. All cathepsins showed similar action patterns, with high levels early on in the aging process and lower levels at later times. This pattern depended on the genotype and was significantly faster (P≤0.05) in meat from mh/mh animals, intermediate in meat from mh/+ animals and slower in meat from normal (+/+) animals of both breeds. Copyright © 2006 Society of Chemical Industry
Meat Science, 1990
A BSTRA CT A series of experiments was conducted in an attempt to immunohistochemicalh' ident([~v specific musch" proteins #t raw bovine muscle, meat hatters and .fineO" conuninuted meat pro~htcts. Three different antibodies were investigated-monoclonal anti-actin (IgG), poO,clonal anti-desmh~ (IgG) and polyclonal anti-myoglobin (IgM). In addition, the fluorescent compound nitrobenzooxadiazole (NBD)-phallacidin was tested. The utility of the antibody anti-desmin proved to be poor. Anti-myoglobin and NBDphallacidin were useful in muscle tissues that had been technologicall.v treated to a limited extent. Anti-actin reacted with actin present in raw muscle tissue, in muscle samples commhtuted with and without additives and in muscle samples that had been comminuted with additives and subsequently heated to 80"~C and 115 ~ C. However, its reaetivi O' was markedly more disthwt #r raw than ht processed samples. The utility oj current immunohistochenfical techniques to study the microstructure of processed meats seems to be limited due to the rapid denaturation of the specific muscle proteins.
Journal of Food Biochemistry, 2007
The objective of this study was to elucidate a relationship between some endogenous proteinases and their inhibitors in four diflerent goat muscles during postmortem storage. Samples were taken porn the longissimus dorsi (D), biceps femris (Bm, semimmbranosus (SM) and semitendinosus (ST) muscles stored up to 20 days postmortem at 5C. Activities of calpain-I, calpain-II, calpastatin, cathepsins (B, B+L, H and D) and cystatin(s) were detemhed. Decreases in calpain-I andcalpastatin activities were significantly more than that of calpain-11 activity. The cathepsin B, B+L, H and cystatin level were found to fail by 9-35 % after 20 days, whereas the cathepsin D showed 11-I 7% decline in all ihe muscles. Thus changes in muscle proteinases and their inhibitors during postmortem storage difler and the results may shed light on their role in myofibrillar proteolysis and goat meat tenderization.
Aminopeptidase interference in the assay of muscle cathepsin H
Journal of the Science of Food and Agriculture, 1991
Muscle cathepsin H is usually assayed with L-arginine 7-(4-methyl)coumarylamide but exopeptidase activities may interfere. Only 4-4'5% of the observed substrate hydrolysis when assaying cathepsin H has been found to be due to muscle aminopep tidases .
Evaluation of cathepsin B levels in fresh thighs selected for cured raw ham production
Meat Science, 1997
Excessive meat tenderization in cured raw Parma ham has recently been correlated with abnormal levels of cathepsin B in freshIy slaughtered thigh meat. We have developed a visual assay employing the substrate Z-Arg-Arg-NNapOMe for the quantitative detection of active cathepsin B levels in pork thigh muscle homogenates. The work was based on a kinetic characterization, in steady state condition, of pig muscle cathepsin B with several peptidyl chromophoric substrate analogs. This assay can easiIy and safely be performed by non-specialized personnel directly in the slaughterhouse or in the factory, for an earIy quality evaluation of thighs selected for Parma ham production. Our characterization has further indicated that the catalytic properties of porcine muscle cathepsin B and those of isoforms from other animal and plant species are practically identical. This is particularly evident in the commercially available bovine spleen isoform, which was employed as a model enzyme in most of the experiments.