The study examined the protein profile of Pectoralis major muscle in broiler chickens subjected to different freezing and thawing methods. Pectoralis major muscle was excised from the carcasses of twenty broiler chickens and split into left and right halves. The left half was subjected to slow freezing (-20oC) while the right half was rapidly frozen (-80oC). The samples were stored at their respective temperature for 2 weeks and assigned to either of tap water (27oC, 30 min), room temperature (26oC, 60 min), microwave (750W, 10 min) or chiller (4oC, 6 h) thawing. Changes in myofibrillar proteins following the thawing methods were monitored through sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The electrophoretic profile indicated differences (p < 0.05) in intensities of the components of myofibrillar proteins among the thawing methods in both slow and rapidly frozen samples. Chiller thawing had significantly higher (p < 0.05) protein concentration than other methods in rapidly frozen samples. However, in slow freezing, there were no significant differences in protein concentration among the thawing methods. In rapidly frozen samples, the protein optical densities at molecular weight of 21, 27, 55 and 151kDa in tap water, chiller and room temperature thawing did not differ (p < 0.05). Similarly, in slowly frozen samples, protein optical densities at molecular weight of 21, 27, 85 and 151 kDa were not significantly different among chill, tap water and room temperature thawing. Microwave thawing consistently caused higher protein degradation resulting in significantly lower (p < 0.05) protein quality and quantity in both freezing methods.
Different heat treatments, (1) chilled, 4°C (2) boiled at 100°C for 30 min and (3) autoclaved at 121°C at 15 psi for 20 min were employed on goat meat to mimic domestic and industrial cooking. The effects on intensity of actin proteins was observed using two-dimensional gel electrophoresis where significant differences (p>0.05) were observed in the spot intensity between chilled and boiled samples, similarly in chilled and autoclaved samples. However, no significant difference was observed between boiled and autoclaved samples. The slight changes observed in the cooking of meat confirmed that actin protein is susceptible to denaturation cause by heat. MALDI-TOF/TOF analysis revealed the peptide-mass fingerprint between positions 21 – 374 that not affected by heat treatment. Peptides from this position merit the candidature of actin as putative thermostable marker for detecting goat meat (chevon) in food product.
The properties of collagens from Barramundi (Lates calcarifer) skin obtained by acid solubilized (control), pepsin and papain aided extractions were investigated. The yields of collagens (dry weight basis) for acid solubilized, pepsin and papain aided extractions were 8.1, 43.6 and 44.0%, respectively. The collagens were generally colorless although collagens from the enzymes aided-extractions were slightly darker. Based on the e-nose evaluation, the collagens were considered odorless. The pH of all the collagens was in the vicinity of 3; however, those extracted with papain had significantly higher pH. The polypeptide profiles obtained in the SDS-PAGE analysis for pepsin extracted collagen were similar to those of acid solubilized collagens. Papain extracted collagen had distinctly different SDS-PAGE pattern. All the extracted collagens were of type 1 with apparent peptides molecular weight distribution of 37 to 250 kDalton. They had high solubility in pH 2 to 5 and increasing NaCl concentration up to 6%.
This study evaluated the effects of Averrhoa bilimbi juice extract and storage temperature
on lipid oxidation and microbial spoilage of spent chicken meat. Ten, 80 weeks old spent
chickens were slaughtered, eviscerated and aged for 24 h at 4oC. Thereafter, the Pectoralis
major muscles and right thighs were excised and marinated in either A. bilimbi juice extract,
pure distilled water, or no marination (control) for either 4 or 9 h at room temperature or 9 or 24
h at 4°C. Lipid oxidation was monitored on the Pectoralis major muscles while the right thighs
were assessed for Enterobacteriacea counts. Lipid oxidation was not significantly affected
by the type or duration of marination. Marination showed a temperature dependent effect on
Enterobacteriacea counts. At room temperature, samples that were marinated by distilled water
showed significantly higher Enterobacteriacea counts than the control while those that were
marinated with A. bilimbi juice extract showed no growth at both 4 and 9 h of marination. At
chilled temperature, marination had no significant effects on the growth of Enterobacteriacea
during the 9 or 24 h storage. These results indicated that A. bilimbi juice extract marinade has
some antibacterial activities but works better when combined with refrigerated storage.