The major fish allergen, parvalbumin, is a low-molecular-weight (10 to 13 kDa), heat-stable protein. Monoclonal antibody (MAb) 3E1, developed against heat-treated catfish sarcoplasmic protein extract, recognizes a thermal-stable protein with the molecular-weight range of parvalbumin in fish extracts. We further investigated the antigen-binding characteristics of this antibody by comparing its immunoreactivity against various fish and other animal species, with a commercially available anti-parvalbumin antibody, MAb PARV-19. Soluble proteins were extracted from 67 cooked (100 degrees C for 20 min) finfish, shellfish, meat, and poultry species. Indirect enzyme-linked immunosorbent assay (ELISA) was performed to examine the immunoreactivity of both MAb 3E1 and MAb PARV-19 with sample extracts. Western blot was performed to compare the antigenic protein banding patterns in cooked fish extracts by using these two MAbs. The ELISA results revealed that both MAbs had identical reaction patterns to the fish species tested. Removal of Ca2+ from the fish extracts increased the overall immunoreactivity of both MAbs. Western blot results confirmed that the antigenic protein banding pattern in various fish species blotted by MAb 3E1 corresponded to the molecular weights of parvalbumins recognized by PARV-19. However, screening with non-finfish extracts revealed MAb 3E1 to be strictly finfish specific, while PARV-19 cross-reacted with frog, rat, and rabbit extracts. Based on the heat stability, molecular weight, immunoreactivity, and Ca2+-dependent binding of the antigenic proteins, MAb 3E1 is specific to fish parvalbumin. It would therefore be a useful probe for investigating the major fish allergen in both raw and processed food.

Pangasius catfish, primarily tra (Pangasius hypophthalmus) and basa (Pangasius bocourti), are farm-raised catfish imported from Asia and have become a common substitute for domestic catfish, grouper, and other high-valued fish in restaurant-served dishes in the United States. This article reports on the development of a monoclonal antibody-based sandwich enzyme-linked immunosorbent assay (ELISA) for the identification of cooked Pangasius fish, basa, and tra. The assay uses a pair of monoclonal antibodies (MAbs F7B8 and T7E10) specific to a heat-stable 36-kDa protein present in a saline extraction of the fish muscle; MAb F7B8, which cross-reacts to all fish species, is the capture antibody and the biotin-conjugated MAb T7E10, which is specific to Pangasius fish, is the detection antibody. This sandwich ELISA reliably identified fully cooked basa and tra from more than 70 common finfish, shellfish, land animal species, and other protein materials tested. It can also sensitively detect 0.5% of adulterated basa or 0.1% tra in a mixed crabmeat products with low intra-assay (%CV: 2.59 to 4.14) and inter-assay (%CV: 3.36 to 3.71) variabilities. The new assay provides a rapid and reliable means of distinguishing fish in the Pangasiidae family from other common food fish and nonfish species and will greatly assist efforts to discourage the illegal practice of substituting high-value popular fish species by the cheaper farm-raised imported Pangasius fish at the retail and restaurant levels.

Currently no rapid immunoassays are developed to identify the species content of fat tissue in mixtures. We report a simple protocol enabling the effective detection of bovine fat in highly processed materials using a lateral flow (LF) immunoassay which targets a ruminant‐specific muscle protein. A portion (50 gm) of muscle‐free fat samples was rendered to separate the molten fat from the proteinaceous residue, then soluble proteins were extracted from the solid residue with 0.5 mol/L NaCl for the LF analysis. The assay could detect 2% bovine fat‐in‐pork fat, 1% bovine fat‐in‐porcine meat‐and‐bone meal, and 0.5% bovine fat‐in‐soy meal mixtures. Rendered bovine fat could be detected up to 213°C. These results demonstrate that low levels of bovine fat tissue can be detected in processed materials using an immunoassay based on the presence of the muscle protein which serves as a species marker in the fat tissue.

Four IgG (subclass IgG1) class monoclonal antibodies (MAbs) strongly reactive to Asian farm-raised Pangasius catfish, tra (Pangasius hypophthalmus) and basa (Pangasius bocourti), have been developed. These MAbs were raised by immunizing an animal with thermal-stable crude sarcoplasmic protein extract of cooked tra. The MAbs were selected by screening hybridoma clones against more than 70 common fish and meat protein extracts. Two MAbs, T7E10 and T1G11, were found to be specific to the Asian Pangasius catfish, tra, and basa, with no cross-reactions with any of the common fish and meat species or with the food additive proteins (bovine serum albumin, soy proteins, milk proteins, egg proteins, and gelatin) tested. MAb T7E10 recognized 2 antigenic proteins (molecular weight approximately 36 and 75 kDa) in raw and cooked tra and basa extracts, while T1G11 bound to several proteins (molecular weight between 13 and 18 kDa) in tra and basa extracts. Two other MAbs, F7B8 and F1G11, recognized a common protein (36 KDa) and cross-reacted with all the fish extracts tested and with several mammalian species. These MAbs can be employed individually or in combination in various formats of immunoassays for rapid identification of Pangasius catfish, either raw or cooked. They can also be used to study the biological, biochemical, and physiological aspects of thermal-stable antigenic proteins. This is the first study identifying these thermal-stable antigenic proteins present in Pangasius catfish as species-specific biomarkers.

Zdrowie i życie ludzkie to wartości, którym ponad wszelką wątpliwość należy przypisać szczególne znaczenie. Znajduje to swoje odbicie na wielu płaszczyznach - również na gruncie systemu prawnego, który zapewnia im szczególną ochronę, która uwidacznia się w każdej pojedynczej gałęzi prawa. Autorzy swoje rozważania przenieśli na grunt prawa pracy, gdzie gwarantem ochrony zdrowia i życia ludzkiego uczyniony został pracodawca, w związku z czym ciąży na nim szereg doniosłych obowiązków, a ich niedopełnienie wiąże się z koniecznością zastosowania sankcji karnej. To czyni rozważania Autorów interdyscyplinarnymi. Autorzy wskazują, że nawet zdarzenia nagłe, nieprzewidziane i nadzwyczajne nie zwalniają pracodawcy z obowiązku zapewnienia ochrony zdrowia i życia pracowników podczas wykonywania przez nich pracy. Tematem rozważań Autorów uczyniona została problematyka ochrony zdrowia i życia pracowników, przy czym rozważania te mają swój konkretny kontekst. Jest to pandemia wirusa SARS-CoV-2, który jest największym zagrożeniem zdrowia i życia, z jakim obecnie przyszło się zmierzyć - również pracownikom i pracodawcom. Wiąże się z tym konieczność wdrożenia odpowiednich procedur, a także określonych zachowań, na które wskazują Autorzy w swoim opracowaniu. Wreszcie - Autorzy opisują również prawnokarne konsekwencje niedopełnienia przez pracodawcę obowiązku ochrony zdrowia i życia pracowników w nadzwyczajnym czasie pandemii.