Development of an integrated model for heat transfer and dynamic growth of Clostridium perfringens during the cooling of cooked boneless ham.

Numerous small meat processors in the United States have difficulties complying with the stabilization performance standards for preventing growth of Clostridium perfringens by 1 log10 cycle during cooling of ready-to-eat (RTE) products. These standards were established by the Food Safety and Inspection Service (FSIS) of the US Department of Agriculture in 1999. In recent years, several attempts have been made to develop predictive models for growth of C. perfringens within the range of cooling temperatures included in the FSIS standards. Those studies mainly focused on microbiological aspects, using hypothesized cooling rates. Conversely, studies dealing with heat transfer models to predict cooling rates in meat products do not address microbial growth. Integration of heat transfer relationships with C. perfringens growth relationships during cooling of meat products has been very limited. Therefore, a computer simulation scheme was developed to analyze heat transfer phenomena and temperature-dependent C. perfringens growth during cooling of cooked boneless cured ham. The temperature history of ham was predicted using a finite element heat diffusion model. Validation of heat transfer predictions used experimental data collected in commercial meat-processing facilities. For C. perfringens growth, a dynamic model was developed using Baranyi's nonautonomous differential equation. The bacterium's growth model was integrated into the computer program using predicted temperature histories as input values. For cooling cooked hams from 66.6 degrees C to 4.4 degrees C using forced air, the maximum deviation between predicted and experimental core temperature data was 2.54 degrees C. Predicted C. perfringens growth curves obtained from dynamic modeling showed good agreement with validated results for three different cooling scenarios. Mean absolute values of relative errors were below 6%, and deviations between predicted and experimental cell counts were within 0.37 log10 CFU/g. For a cooling process which was in exact compliance with the FSIS stabilization performance standards, a mean net growth of 1.37 log10 CFU/g was predicted. This study introduced the combination of engineering modeling and microbiological modeling as a useful quantitative tool for general food safety applications, such as risk assessment and hazard analysis and critical control points (HACCP) plans.

Validation of acid washes as critical control points in hazard analysis and critical control point systems.

A 2% lactic acid wash used in a large meat-processing facility was validated as an effective critical control point (CCP) in a hazard analysis and critical control point (HACCP) plan. We examined the microbial profiles of beef carcasses before the acid wash, beef carcasses immediately after the acid wash, beef carcasses 24 h after the acid wash, beef subprimal cuts from the acid-washed carcasses, and on ground beef made from acid-washed carcasses. Total mesophilic, psychrotrophic, coliforms, generic Escherichia coli, lactic acid bacteria, pseudomonads, and acid-tolerant microorganisms were enumerated on all samples. The presence of Salmonella spp. was also determined. Acid washing significantly reduced all counts except for pseudomonads that were present at very low numbers before acid washing. All other counts continued to stay significantly lower (P < 0.05) than those on pre-acid-washed carcasses throughout all processing steps. Total bacteria, coliforms, and generic E. coli enumerated on ground beef samples were more than 1 log cycle lower than those reported in the U.S. Department of Agriculture Baseline data. This study suggests that acid washes may be effective CCPs in HACCP plans and can significantly reduce the total number of microorganisms present on the carcass and during further processing.

Proportion of types I and III collagen in longissimus collagen from bulls and steers.

The proportion of types I and III intramuscular collagen in longissimus muscles of Simmental bulls (n = 8) and steers (n = 8) 17 mo of age was studied. Longissimus samples taken 7 d after slaughter were evaluated for total collagen, types I and III collagen, heat-soluble collagen, sensory panel traits and Warner-Bratzler shear force. Intramuscular collagen (IMC) was isolated and digested with cyanogen bromide, and peptides were resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Percentage of type III IMC was calculated from the total of types I and III collagen as determined from the peak area of densitometric scans of the cyanogen bromide peptides alpha 1(I)CB8 and alpha 1(III)CB8. Longissimus muscles from steers had lower (P less than .05) Warner-Bratzler shear values, less (P less than .05) sensory panel-detectable connective tissue and more (P less than .05) tender panel ratings for muscle fiber tenderness and overall tenderness. Muscles from steers had more (P less than .05) heat-soluble collagen than those from bulls, but no differences (P greater than .05) were found for total collagen and percentage of type III collagen. Some intramuscular-collagen characteristics may have contributed to the less tender muscle of bulls. However, the proportion of types I and III collagen did not account entirely for the tenderness difference between steer and bull muscles. Because there were differences in collagen solubility in muscles from steers and bulls, other collagen characteristics such as crosslinking or fiber size may have been more important than collagen type.

Heat-induced changes in the proportion of types I and III collagen in bovine Longissimus dorsi.

Intramuscular collagen (IMC) was isolated from the Longissimus dorsi of six Simmental bulls, 17 months of age, to evaluate the effect of heating on the proportion of types I and III collagen. Cyanogen bromide (CNBr) peptides were prepared from unheated IMC and the soluble and insoluble fractions of IMC heated to 70°C for 70 min or 90°C for 140 min. Percentage of type III collagen was determined by densitometric scans of the CNBr peptides, αl(I)CB8 and αl(III)CB8, as resolved by SDS-PAGE. Percentage of collagen solubilized was greater (P < 0·05) at 90°C than at 70°C. The 70°C and 90°C insoluble IMCs were similar (P > 0·05) for percentage of type III, but both had a greater (P < 0·05) percentage of type III than unheated IMC, indicating that type I is more heat labile than type III. Heat-soluble IMC contained both α and ß components and the CNBr peptides of 70°C soluble IMC were mostly type I. These results indicated that heating intramuscular collagen from bulls mainly solubilized type I collagen. Improved tenderness associated with increased heat solubility of collagen may be more closely related to heat-induced solubilization of type I than of type III collagen.