Production of several extracellular virulence factors (lipase, protease and haemolysin) was compared in 15 Aeromonas spp. isolated from faeces of patients with Aeromonas-associated gastroenteritis and 81 strains isolated from food. Strains from food did not show differences in production of these factors when compared with strains isolated from faeces. However, if strains were considered in relation to autoagglutination (AA) character, the AA+ differed from AA- strains in lipase and protease production. Supernatant fluids of AA+ food and human strains showed 2.5-fold more protease production than that observed in AA- strains. These two characteristics of certain Aeromonas strains could be related with the more virulent capacity.
Starch ampicillin agar (SA), starch glutamate ampicillin penicillin agar (SGAP) and Aeromonas medium (AM) were evaluated for enumeration of Aeromonas spp. from foods. Recovery from pure cultures of Aer. hydrophila and Aer. caviae was excellent on all media. Recovery of Aer. sobria was best on AM agar, where 95.5% were recovered, compared with 31.9% on SA agar and 33.3% on SGAP medium.
Immunoelectrophoresis in agarose gels has been used to detect and partially characterise specific protein precipitin bands of beef proteins (CSP), free of cross-reactions with proteins of pig (PSP) and horse (HSP). Out of the six precipitin bands obtained by reacting CSPs against an anti-CSP antiserum produced by a rabbit, only one band was produced by interaction of the anti-CSP antiserum with PSP and HSP. The other five bands were specific beef muscle soluble proteins. This technique may be useful in detecting the presence of beef in unheated ground meat products.
A double-antibody sandwich ELISA (enzyme-linked immunosorbent assay) has been successfully developed for the detection of low levels of chicken meat (1-30%) in unheated meat mixtures. The assay uses chicken-specific antibodies, obtained by immunoadsorption of the crude chicken antisera onto immobilized sarcoplasmic extracts from beef, pig and horse, to remove cross-reacting antibodies. The purified antibodies, bound to the wells of a microtitre plate, sequester chicken muscle soluble proteins from saline extracts of meat mixtures. Immuno-recognition is made with similar purified antibodies conjugated to the enzyme horseradish peroxidase. Subsequent enzymic conversion of substrate gives clear optical density differences, when assaying minced beef and pig containing variable amounts of chicken meat.
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