Youling L. Xiong

Antimicrobial activities of spice extracts against pathogenic and spoilage bacteria in modified atmosphere packaged fresh pork and vacuum packaged ham slices stored at 4 °C

The antimicrobial activity of 14 spice extracts against four common meat spoilage and pathogenic bacteria (Listeria monocytogenes, Escherichia coli, Pseudomonas fluorescens and Lactobacillus sake) was screened in cultured media (experiment 1). The results showed that individual extracts of clove, rosemary, cassia bark and liquorice contained strong antimicrobial activity, but the mixture of rosemary and liquorice extracts was the best inhibitor against all four types of microbes. Subsequently, mixed rosemary/liquorice extracts were spray-applied to inoculated fresh pork in modified atmosphere packaging (experiment 2) and to inoculated ham slices in vacuum packaging (experiment 3). The meat samples were stored at 4°C over a 28-day period and microbial growth was monitored regularly. The L. monocytogenes population on fresh pork by day 28 decreased 2.9, 3.1 and 3.6 logs, the MAB decreased 2.7, 2.9 and 3.1 logs, the Pseudomonas spp. count decreased 1.6, 2.1 and 2.6 logs and the total coliform count decreased 0.6, 0.8 and 1.2 logs, corresponding to 2.5, 5.0 and 10.0mg/ml of spray, respectively, when compared to control (P<0.05). The number of L. monocytogenes on ham slices decreased 2.5, 2.6 and 3.0 logs, the MAB plate counts decreased 2.9, 3.0 and 3.2 logs and the LAB counts decreased 2.4, 2.6 and 2.8 logs (P<0.05), respectively, after 28-days, by the same levels of mixed rosemary/liquorice extract treatments. The results demonstrated strong potential of mixed rosemary and liquorice as a natural preservative in fresh pork and ham products.

Myofibrillar protein from different muscle fiber types: Implications of biochemical and functional properties in meat processing∗

Texture, moisture retention, and tenderness of processed muscle foods are influenced by the functionality of myofibrillar protein. Recent studies have revealed large variations in processing quality between red and white muscle groups that can be attributed to differences in the functional properties of myofibrillar protein associated with the type of fiber. Myofibrillar proteins from fast- and slow-twitch fibers exhibit different biochemical and rheological characteristics and form gels with distinctly different viscoelastic properties and microstructures. The existence and wide distribution of the numerous myosin isoforms in different muscle and fiber types contribute to the various functional behaviors of myofibrillar protein. The different sensitivities of fast and slow myofibrillar proteins to pH, ionic environment, temperature, and other external factors have been well documented and illustrate the importance of adjusting meat processing conditions, according to fiber type profile to achieve maximum protein functionalities, and hence, uniform quality of the final muscle foods.

Structural and Emulsifying Properties of Soy Protein Isolate Subjected to Acid and Alkaline pH-Shifting Processes

Structural unfolding of soy protein isolate (SPI) as induced by holding (0, 0.5, 1, 2, and 4 h) in acidic (pH 1.5-3.5) and alkaline (pH 10.0-12.0) pH solutions, followed by refolding (1 h) at pH 7.0, was analyzed. Changes in emulsifying properties of treated SPI were then examined. The pH-shifting treatments resulted in a substantial increase in protein surface hydrophobicity, intrinsic tryptophan fluorescence intensity, and disulfide-mediated aggregation, along with the exposure of tyrosine. After the pH-shifting processes, soy protein adopted a molten globule-like conformation that largely maintained the original secondary structure and overall compactness but lost some tertiary structure. These structural modifications, consequently, led to markedly improved emulsifying activity of SPI as well as the emulsion stability.

Variation in the cross-linking pattern of porcine myofibrillar protein exposed to three oxidative environments.

Myofibrillar protein (MP, 26 mg protein/mL in 0.6 M NaCl, pH 6.0) prepared from pork serratus ventralis muscle was incubated at 4 degrees C for 24 h with three oxidizing systems: (1) an iron-catalyzed oxidizing system (IOS: 10 microM FeCl(3), 0.1 mM ascorbic acid, and 0.05-5.0 mM H(2)O(2)), (2) a linoleic acid-oxidizing system (LOS: 0.05-5.0 mM linoleic acid and 3750 units of lipoxidase/mL), or (3) a H(2)O(2)-activated metmyoglobin-oxidizing system (MOS: 0.05-0.5 mM metmyoglobin/ H(2)O(2)). Oxidation in IOS and MOS promoted extensive, dose-dependent cross-linking and insolublization of MP, notably myosin, while the effect of LOS was minimal. Chymotrypsin digestion indicated that the rod (tail) subfragment of myosin was the preferred target of hydroxyl radicals and ferryl oxygen species, although the s-1 (head) region was also susceptible. Disulfide bonds were responsible for most of the cross-linking, and malonaldehyde appeared to contribute to the cross-linking as well. However, dityrosine was minimally involved. Overall, the systems that generate hydroxyl radicals and ferryl oxygen species were more potent than the system that produces peroxide in the cross-linking and aggregation of MP; such covalent links were implicated in the functionality changes of low-temperature-processed muscle foods.

Hydroxyl Radical and Ferryl‐Generating Systems Promote Gel Network Formation of Myofibrillar Protein

UNLABELLED The objective of the study was to examine how oxidatively induced protein cross-linking would influence the gelation properties of myofibrillar protein (MP) under meat processing conditions. MP suspensions in 0.6 M NaCl at pH 6 were treated with an iron-catalyzed oxidizing system (IOS: 10 microM FeCl(3), 0.1 mM ascorbic acid, 0.05 to 5 mM H(2)O(2)) or a H(2)O(2)-activated metmyoglobin oxidizing system (MOS: 0.01 to 0.1 mM metmyoglobin/H(2)O(2)) that produced hydroxyl radical and ferryl species, respectively. Both oxidizing systems promoted MP thermal gelation, which was evidenced by rapid protein-protein interaction and the enhancement in storage modulus (elasticity) of the gel network as revealed by dynamic rheological testing in the 20 to 74 degrees C temperature range. This gelation-enhancing effect was attributed to the shift of myosin aggregation in the early stage of heating from predominantly head-head association (nonoxidized control samples) to prevalently tail-tail cross-linking through disulfide bonds. However, both hardness and water-holding capacity of chilled gels tended to decline when MP was exposed to >or=1 mM H(2)O(2) in IOS and to all concentrations of metmyoglobin in MOS. Microscopic examination confirmed a more porous structure in oxidized gels when compared with nonoxidized protein gels. The results demonstrated that mild oxidation altered the mode of myosin aggregation in favor of an elastic gel network formation, but it did not improve or had a negative effect on water-binding properties of MP gels. PRACTICAL APPLICATION Mild oxidation promotes protein network formation and enhances gelation of myofibrillar protein under normal salt and pH conditions used in meat processing. This oxidative effect, which involves disulfide linkages, is somewhat similar to that in bakery product processing where oxidants are used to improve dough performance through gluten protein interaction.

Effect of dietary ractopamine on tenderness and postmortem protein degradation of pork muscle

Twenty-four finishing pigs with a mean starting weight of 82kg were assigned to two dietary regimens: (1) a corn-soybean meal basal diet (control; n=12), and (2) the basal diet supplemented with 20ppm ractopamine HCl (RAC; n=12). After 28-30 days on the feeding trial, pigs were slaughtered, and the growth and carcass characteristics were measured. Furthermore, the 3rd-13th rib section of longissimus muscle was excised at 48h postmortem, sliced into 19-mm thick chops, vacuum packaged, stored at 2°C, and subjected to Warner-Bratzler shear force (WBSF) and electrophoretic tests after 2, 4, 7, 10, 14, and 21 days (postmortem). RAC feeding increased (P<0.01) pig carcass weight and percent lean, but it also increased the day-2 muscle WBSF by 20% (P<0.01). The shear force difference between control and RAC pig muscles gradually decreased and vanished by day 10 (P>0.05) when both muscle groups became more tender. The muscle from RAC-fed pigs exhibited a slower protein degradation rate than muscle from the control animals, notably for proteins in the 15-45kDa range. The results suggested that the tenderness difference between ractopamine-treated and control pig muscles was related to the proteolysis rate, and could be diminished with adequate postmortem ageing.

Antioxidant activity of spice extracts in a liposome system and in cooked pork patties and the possible mode of action

Three experiments were conducted to assess the antioxidant efficacy of spice extracts in cooked meat. In experiment 1, antioxidant activity of 13 common spice extracts was screened in a liposome system. Six of the extracts (clove, rosemary, cassia bark, liquorice, nutmeg, and round cardamom), identified to have the greatest total phenolic contents, were strongly inhibitory of TBARS formation. In experiment 2, 2,2-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity, ferric-reducing power, and metal chelation of these six spice extracts were evaluated. Clove exhibited the greatest reducing power, and all had strong DPPH scavenging activity. In experiment 3, clove, rosemary, and cassia bark extracts were further tested for in situ antioxidant efficacy. Cooked pork patties containing these spice extracts had markedly reduced TBARS formation and off-flavour scores but a more stable red colour, during storage. The results demonstrated strong potential of spice extracts as natural antioxidants in cooked pork products.

Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein.

The effect of chlorogenic acid (CA) at different concentration levels (0, 6, 30, and 150 μmol/g protein) on porcine myofibrillar protein (MP) gelling potential in relation to chemical and structural changes was investigated. The results showed that CA generally inhibited protein carbonyl formation but did not prevent sulphydryl and amine losses caused by oxidation. The presence of CA intensified oxidation-initiated loss of α-helix conformation as well as tertiary structure of MP. CA at 150 μmol/g produced the greatest increase in MP surface hydrophobicity and insolubility. The physicochemical changes with 6 and 30 μmol/g CA led to a remarkably enhanced gelling capacity of MP and augmented the positive effect of oxidation in building an elastic gel network. However, CA at 150 μmol/g was detrimental to the MP gelation. The result can explain why processed meats with phenolic-rich spices and herbs often exhibit variable texture-forming properties.

Production of cured meat color in nitrite-free Harbin red sausage by Lactobacillus fermentum fermentation

Lactobacillus fermentum was substituted for nitrite to produce cured pink color in a Chinese-style sausage. Treatments included inoculations (10(4), 10(6), and 10(8)CFU/g meat) followed by fermentation at 30°C for 8h and then at 4°C for 16h. Control sausage (with sodium nitrite, 60mg/kg meat) was cured at 4°C for 24h without L. fermentum. The UV-Vis spectra of pigment extract from L. fermentum-treated sausage were identical to that of nitrosylmyoglobin (NO-Mb) formed in nitrite-treated control. The NO-Mb concentration and the colorimetric a(∗) value of sausage treated with 10(8)CFU/g meat of L. fermentum essentially replicated those in nitrite-cured meat. Free amino acid content in sausage treated with L. fermentum was greater and the pH slightly lower compared with the nitrite-cured control sample. This study showed that L. fermentum has the potential to substitute for nitrite in the sausage production.

Protein Oxidation Enhances Hydration but Suppresses Water-Holding Capacity in Porcine Longissimus Muscle

Pork longissimus muscle was oxidized at 4 °C by mixed 10 μM FeCl(3)/100 μM ascorbate with 1, 5, 10, 20, 30, 40, or 50 mM H(2)O(2) (pH 6.2). Oxidation with >1 mM H(2)O(2) for 40 min significantly (P < 0.05) enhanced hydration of muscle samples, whereas oxidation with 40 and 50 mM H(2)O(2) for 2 min or with 20 mM H(2)O(2) for 40 min caused pronounced declines in water-holding capacity and product yield. The changes coincided with marked increases in the protein carbonyl content, TBARS formation, and cross-linking of both myofibrillar and sarcoplasmic proteins. Dye-tracing tests showed that the enhanced hydration at >1 mM H(2)O(2) was due to facilitated water diffusion into muscle tissue. This result was strongly corroborated by microscopic images that illustrated enlargements of intercellular spacing, that is, gaps, in oxidized muscle tissue, which served as canals for water diffusion.