Composition and toxigenic potential of the mould population on dry-cured Iberian ham

Núñez, Félix; Rodrı́guez, Mar; Bermúdez, Elena; Córdoba, Juan J.; Asensio, Miguel A.

doi:10.1016/0168-1605(96)01126-9

Cited by 141 publications

(65 citation statements)

References 25 publications

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“…These proteins are hydrolyzed in dry-cured ham during the drying stage (4), when P. chrysogenum reaches counts of about 10 7 CFU/g (18). On the other hand, myoglobin was not affected by EPg222.…”

Section: Discussionmentioning

confidence: 99%

“…This medium was developed to simulate the conditions for nitrogen source, NaCl concentration, and pH that P. chrysogenum Pg222 finds on dry-cured ham at the first stages of processing (4,18,22).…”

Section: Discussionmentioning

confidence: 99%

“…The strain Pg222 of P. chrysogenum, isolated from dry-cured ham (18) and showing a high proteolytic activity (13), was used in this study.…”

Section: Methodsmentioning

confidence: 99%

“…During this time, an uncontrolled microbial population grows on the surface (18). Molds, yeasts, and gram-positive catalase-positive cocci have been reported as the dominant organisms on the surface of dry-cured ham (17,18,22). Most molds and some cocci growing spontaneously on dry-cured ham are toxigenic (18,23).…”

mentioning

confidence: 99%

“…Molds, yeasts, and gram-positive catalase-positive cocci have been reported as the dominant organisms on the surface of dry-cured ham (17,18,22). Most molds and some cocci growing spontaneously on dry-cured ham are toxigenic (18,23). However, they show an interesting hydrolytic activity on myofibrillar proteins, particularly molds (13,14).…”

mentioning

confidence: 99%

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Purification and Characterization of an Extracellular Protease from Penicillium chrysogenum Pg222 Active against Meat Proteins

Benito

Rodrı́guez

Núñez

et al. 2002

Appl Environ Microbiol

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An extracellular protease from Penicillium chrysogenum (Pg222) isolated from dry-cured ham has been purified. The purification procedure involved several steps: ammonium sulfate precipitation, ion-exchange chromatography, filtration, and separation by high-performance liquid chromatography. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis and gel filtration, the purified fraction showed a molecular mass of about 35 kDa. The hydrolytic properties of the purified enzyme (EPg222) on extracted pork myofibrillar proteins under several conditions were evaluated by SDS-PAGE. EPg222 showed activity in the range of 10 to 60°C in temperature, 0 to 3 M NaCl, and pH 5 to 7, with maximum activity at pH 6, 45°C, and 0.25 M NaCl. Under these conditions the enzyme was most active against tropomyosin, actin, and myosin. EPg222 showed collagenolytic activity but did not hydrolyze myoglobin. EPg222 showed higher activity than other proteolytic enzymes like papain, trypsin, and Aspergillus oryzae protease. The N-terminal amino acid sequence was determined and was found to be Glu-Asn-Pro-Leu-Gln-Pro-Asn-Ala-Pro-Ser-Trp. This partial amino acid sequence revealed a 55% homology with serine proteases from Penicillium citrinum. The activity of this novel protease may be of interest in ripening and generating the flavor of dry-cured meat products.Dry-cured ham is an uncooked meat product obtained after 8 to 24 months of ripening. During this time, an uncontrolled microbial population grows on the surface (18). Molds, yeasts, and gram-positive catalase-positive cocci have been reported as the dominant organisms on the surface of dry-cured ham (17,18,22). Most molds and some cocci growing spontaneously on dry-cured ham are toxigenic (18, 23). However, they show an interesting hydrolytic activity on myofibrillar proteins, particularly molds (13,14).A decisive role has been attributed to proteolysis in the taste (15) and in the generation of flavor (28) in dry-cured meat products. For this reason, the use of proteolytic molds or their purified enzymes would increase protein hydrolysis in drycured meat products, which is of special interest in shortening their ripening time.Several proteolytic enzymes from fungi and bacteria have been purified and characterized, but only a limited number of proteases from microorganisms isolated from dry-cured meat products have been reported (24). On the other hand, the intracellular cell extract of Penicillium aurantiogriseum isolated from dry-cured meat products has been demonstrated elsewhere to show an increase of proteolysis during the ripening of these products (2). A selected nontoxigenic strain of Penicillium chrysogenum (Pg222) has shown a high proteolytic activity on controlled ripening of pork loins (14), but its proteases have not been characterized. Since these microorganisms are able to grow on dry-cured meat products, with 2 to 4% NaCl and quite restrictive water activity values (4, 22), their proteases could be very efficient at hydrolyzing meat proteins ...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

“…The strain Pg222 of P. chrysogenum, isolated from dry-cured ham (18) and showing a high proteolytic activity (13), was used in this study.…”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Purification and Characterization of an Extracellular Protease from Penicillium chrysogenum Pg222 Active against Meat Proteins

Benito

Rodrı́guez

Núñez

et al. 2002

Appl Environ Microbiol

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Microbial ecology of pork meat and pork products

Iacumin

Carballo

2016

Quantitative Microbiology in Food Processing

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Effect of the fungal protease EPg222 on proteolysis and texture in the dry fermented sausage ‘salchichón’

et al. 2004

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Proteolytic activity of the fungal protease EPg222 and its effect on the texture of the dry fermented sausage 'salchichón', which has a long ripening process, was assayed. Samples with enzyme added showed a significant reduction of myofibrillar protein concentration during the ripening period, compared with a control, and proteolytic activity of the enzyme led to a higher accumulation of non-protein and -amino acid nitrogen. Analysis of volatile compounds in ripened dry fermented sausages revealed that only in EPg222 batches were branched compounds derived from amino acids catabolism detected that are associated with the flavour of dry cured meat products. The texture profile analysis showed reduction in hardness, gumminess and chewiness values in treated compared with control sausages. The effect of this enzyme could be of great interest in stimulating proteolysis, in flavour development and in reducing the hardness of dry fermented sausages produced by a long ripening process.

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Composition and toxigenic potential of the mould population on dry-cured Iberian ham

Cited by 141 publications

References 25 publications

Purification and Characterization of an Extracellular Protease from Penicillium chrysogenum Pg222 Active against Meat Proteins

Purification and Characterization of an Extracellular Protease from Penicillium chrysogenum Pg222 Active against Meat Proteins

Microbial ecology of pork meat and pork products

Effect of the fungal protease EPg222 on proteolysis and texture in the dry fermented sausage ‘salchichón’

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