Investigation of methods to detect mechanically recovered meat in meat products — III: Microscopy

Pickering, Kathleen; Evans, Corinne L.; Hargin, Kevin D.; Stewart, Catriona A.

doi:10.1016/0309-1740(94)00062-c

Cited by 27 publications

(15 citation statements)

References 4 publications

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“…The present results with immunodiffusion analysis indicate the presence of keratan sulfate (derived from cartilage tissue) in MSCM and meat products with MSCM and confirm the previous histometrical observations (Koolmees et al, 1986;Pickering et al, 1995) of cartilage particles present in MSCM. As far as we know this is the first report of detection of keratan sulfate (a glycosaminoglycan specific to cartilage) in MSCM and meat products containing MSCM.…”

Section: Resultssupporting

confidence: 94%

“…Previous studies (Branscheid, Judas, & Höreth, 2009;Koolmees, Bijker, van Logtestijin, & TuinstraMelgers, 1986;Pickering, Evans, Hargin, & Stewart, 1995) have shown that MSCM contains cartilage particles. If so, MSCM may contain varying amounts of keratan sulfate, which is a glycosaminoglycan found in the structure of cartilage proteoglycans, aggrecan and fibromodulin (Nakano, Dixon, & Ozimek, 2005).…”

Section: Introductionmentioning

confidence: 97%

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Immunological detection of keratan sulfate in meat products with and without mechanically separated chicken meat

2012

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Section: Resultssupporting

confidence: 94%

Section: Introductionmentioning

confidence: 97%

Immunological detection of keratan sulfate in meat products with and without mechanically separated chicken meat

2012

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“…In the field of meat science and processing, Levieux et al (1995) used an immunological method to evaluate end-point temperature of heated meat products. Pickering et al (1995) developed an ELISA method to differentiate between mechanically deboned chicken and generally deboned chicken using chicken bone marrow proteins as antigen. Competitive ELISA has been used to assess structural changes in myoglobin by physicochemical treatments (Levieux & Levieux, 1996).…”

Section: Discussionmentioning

confidence: 99%

Application of competitive indirect enzyme‐linked immunosorbent assay (Ci‐ELISA) for monitoring the degree of frozen denaturation of bovine myosin

Lee

Park

Kim

et al. 1998

Int J of Food Sci Tech

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The denaturation of myosin on freezing and frozen storage was monitored using competitive indirect enzyme-linked immunosorbent assay (Ci-ELISA) formatted with polyclonal antibodies anti-MWM IgG, anti-S-1 IgG and anti-LMM IgG raised against the antigens (Ags) bovine myosin whole molecules (MWMs), heavy meromyosin S-1 (myosin head part, S-1) and light meromyosin (myosin tail part, LMM) respectively. Beef slices and cuts stored at Ϫ20 ЊC or Ϫ50 ЊC lost immune affinity with all antibodies, in particular anti-LMM IgG. Repeated thawing-refreezing treatment caused more myosin denaturation than simple freezing. Myosin from beef stored at Ϫ20 ЊC was denatured more than that stored at Ϫ50 ЊC. The immune affinities between anti-LMM IgG and thawed samples were similar to those from anti-MWM IgG. We were unable to differentiate reliably between fresh and thawed beef using anti-S-1 IgG. Myosin was denatured by freezing, in particular its tail part (LMM). Figure 1 Electrophoretic depictions of primary ␣-chymotryptic digestion (A), isolated myosin fraction (B) and separated S-1 and LMM (C) on SDS-PAGE with 10% acrylamide. H and HЈ, and L and LЈ indicate high-molecular-weight standard and low-molecular-weight standard respectively. Lane 1 and 2, myosin fractions after gel filtration; 5 and 6, after first digestion; 9 and 10, isolated MWM; 11 and 12, purified S-1 (96 kDa); 13 and 14, LMM (56-59 kDa).(P Ͻ 0.01). The limit of detection was 0.1 g mL Ϫ1 (P Ͻ 0.01). Evaluation of Ci-ELISATo assess specificity of IgG for antigen, we tested cross-reactivities between bovine actin and troponin compounds, and anti-MWM IgG; cross-reactivity of S-1 to anti-LMM IgG; and cross-reactivity of LMM to anti-S-1 IgG. We obtained cross reactivi-ty of 8.36% and 4.28% of anti-MWM IgG for actin and troponin compounds,-respectively; 10.3% of anti-LMM IgG for S-1; and 8.6% of anti-S-1 IgG for LMM. The results of the recovery test for each IgG were about 102% ( Table 1). Changes of immune affinityMyosin whole molecule (MWM) In Expt 1, after 2 months storage at Ϫ20 ЊC, the Monitoring the frozen denaturation of muscle myosin by immunoassay J. Lee et al.

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“…The study of Pickering et al (1995a) focused on the microscopical detection of hyaline cartilage after toluidine blue staining in MSM and in hand deboned meat from beef, pork, lamb, chicken and turkey from different carcase parts. Generally, MSM and hand deboned meat could be distinguished by the occurrence of cartilage particles.…”

Section: Cartilagementioning

confidence: 99%

Scientific Opinion on the public health risks related to mechanically separated meat (MSM) derived from poultry and swine

Hald

Baggesen

2013

EFS2

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The purpose of this assessment was to identify public health risks linked to mechanically separated meat (MSM) types from pork and poultry and compare them with fresh meat, minced meat and meat preparations (non-MSM); and to select, rank and suggest objective measurement methods and values for parameters to distinguish MSM types. Microbial hazards in MSM are expected to be similar to those in non-MSM, although the risk of microbial growth increases with the degree of muscle fibre degradation, thus with the separation pressure. For the distinction between the different types of MSM and non-MSM chemical, histological, molecular, textural and rheological parameters were considered as potential indicators. The analysis of available published data suggested that calcium and, if confirmed cholesterol content, was the only appropriate chemical parameters which could be used to distinguish MSM from non-MSM products. On the basis of published data, a model was developed to derive probabilities for a product to be classified as MSM based on the calcium content. Calcium content of 100 mg/100 g, as specified in the Reg. (EC) No. 2074/2005, corresponds to probability of 93.6% for a product to be classified as MSM, according to the model developed. Calcium content alone does not allow differentiation between low pressure MSM and other meat products, and other validated tests would be necessary. Histological parameters considered include microscopic detection of different tissues and their changes. The latter is a promising method for distinction of MSM types, but further validation is needed. In order to improve methods for MSM identification, specifically designed studies for the collection of data obtained by standardised methods on indicators such as calcium and cholesterol should be undertaken, while studies based on combinations of different parameters could also be useful

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Investigation of methods to detect mechanically recovered meat in meat products — III: Microscopy

Cited by 27 publications

References 4 publications

Immunological detection of keratan sulfate in meat products with and without mechanically separated chicken meat

Immunological detection of keratan sulfate in meat products with and without mechanically separated chicken meat

Application of competitive indirect enzyme‐linked immunosorbent assay (Ci‐ELISA) for monitoring the degree of frozen denaturation of bovine myosin

Scientific Opinion on the public health risks related to mechanically separated meat (MSM) derived from poultry and swine

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