Sensory impact of chemical and natural antimicrobials on poultry products: a review.

Antimicrobial agents are added to poultry products after slaughter to prevent the growth of pathogenic and spoilage microorganisms and to extend the shelf-life of these products. Antimicrobials can be either natural or chemical, which may affect the sensory attributes at elevated concentrations, such as surface color, odor, flavor, taste, and texture of the poultry products. Thus, when selecting antimicrobials for use in poultry processing, it is vital to consider the antimicrobial-induced changes in sensory aspects from the consumers' perspectives. In spite of its importance, there has been no systematic review on the influences of antimicrobials on sensory aspects of poultry products. This paper reviews the major antimicrobial agents used in the poultry processing industry and their effects on sensory aspects of the poultry products.

Identification and methionine analog tolerance of environmental bacterial isolates selected on methionine analog containing medium.

Methionine is the first limiting amino acid in poultry feed. Currently, methionine supplement is synthesized from an expensive chemical process requiring hazardous chemicals. Therefore, the objectives of this study were isolation of methionine producing bacteria from environmental samples and quantification of methionine production in these isolated bacteria. MCGC medium was selected as the isolation medium for methionine-producing bacteria by using Corynebacterium glutamicum ATCC13032 and Escherichia coli ATCC23798 as the positive and negative controls, respectively. Thirty-nine bacterial strains were obtained from environmental samples. Only strains A121, A122, A151 and A181 were able to tolerate up to 0.1% (w/v) of ethionine or norleucine. These isolated strains were identified by sequencing small subunit rRNA genes. The results revealed that bacterial strains A121, A122, A151and A181 were Klebsiella species, Acinetobacter baumannii, A. baumannii and Pseudomonas aeruginosa, respectively. When methionine production in strains A121 and A181 was quantitated, strains A121 and A181 generated methionine up to 31.1 and 124.6 µg/ml, respectively.

Characterization of isolated yeast growth response to methionine analogs.

Methionine is one of the first limiting amino acids in poultry nutrition. The use of methionine-rich natural feed ingredients, such as soybean meal or rapeseed meal may lead to negative environmental consequences. Amino acid supplementation leads to reduced use of protein-rich ingredients. The objectives of this study were isolation of potentially high content methionine-containing yeasts, quantification of methionine content in yeasts and their respective growth response to methionine analogs. Minimal medium was used as the selection medium and the isolation medium of methionine-producing yeasts from yeast collection and environmental samples, respectively. Two yeasts previously collected along with six additional strains isolated from Caucasian kefir grains, air-trapped, cantaloupe, and three soil samples could grow on minimal medium. Only two of the newly isolated strains, K1 and C1, grew in minimal medium supplied with either methionine analogs ethionine or norleucine at 0.5% (w/v). Based on large subunit rRNA sequences, these isolated strains were identified as Pichia udriavzevii/Issatchenkia orientalis. P. kudriavzevii/I. orentalis is a generally recognized as a safe organism. In addition, methionine produced by K1 and C1 yeast hydrolysate yielded 1.3 ± 0.01 and 1.1 ± 0.01 mg g(-1) dry cell. Yeast strain K1 may be suitable as a potential source of methionine for dietary supplements in organic poultry feed but may require growth conditions to further increase their methionine content.

In vivo interactions of MyoD, Id1, and E2A proteins determined by acceptor photobleaching fluorescence resonance energy transfer.

MyoD, a skeletal muscle transcription factor, is rapidly degraded by the ubiquitin-proteasome system. MyoD interacts with ubiquitously expressed E2A or inhibitor of DNA binding (Id) proteins to activate or inhibit transcription, respectively. Furthermore, MyoD has been shown to modulate the ubiquitin-mediated degradation of Id1 and E2A proteins, E12 and E47. The molecular mechanisms governing these events are not clear but are hypothesized to occur via heterodimer formation. Fluorescence resonance energy transfer (FRET) is a technique for evaluation of protein-protein interactions in vivo. Using acceptor photobleaching FRET and chimeric proteins composed of MyoD, Id1, E12, E47, E12(NLS), or MyoD(NLS) and either cyan fluorescent protein or yellow fluorescent protein, we show that each of the wild-type proteins is capable of homodimerization. In addition, heterodimers form between Id1 and E2A proteins, as well as between MyoD and E2A proteins. The Id1:E2A interaction is stronger than the MyoD:E2A interaction, which is consistent with the notion that inhibition of MyoD action occurs by the sequestration of E2A proteins by Id. The stronger interaction of Id1 with E2A may also explain the decrease in the rate of ubiquitin-proteasome degradation of Id1 that is significantly greater than that of MyoD when E2A proteins are abundant. Thus, these studies extend our understanding of the molecular mechanisms of MyoD action.

E12 and E47 modulate cellular localization and proteasome-mediated degradation of MyoD and Id1.

Programs of tissue differentiation are likely controlled by factors regulating gene expression and protein degradation. In muscle, the degradation of the muscle transcription factor MyoD and its inhibitor Id1 occurs via the ubiquitin-proteasome system. E12 and E47, splice products of the E2A gene, interact with MyoD to activate transcription of the muscle program and are also degraded by the ubiquitin-proteasome system (t(1/2) = approximately 6 h). E12 and E47 each contain two regions of basic amino acids, which, when mutated, lead to cytoplasmic accumulation of the proteins. These NLS mutants (E12(NLS), E47(NLS)) are degraded with a half-life similar to the wild-type proteins. In nonmuscle cells, cotransfection of either E12 or E47 with MyoD extended MyoD's half-life from approximately 1 to approximately 4 h. In addition, cotransfection of either E12 or E47 with Id1 led to a marked reduction in Id1's degradation rate from t(1/2) of approximately 1 to approximately 8 h. Furthermore, the cotransfection of NLS deficient mutants of MyoD or Id1 with E12 or E47 resulted in altered intracellular localization of the proteins largely dependent upon the E12 or E47 moiety. Cotransfection of wild-type MyoD or Id1 with NLS deficient mutants of E12 or E47 also led to an altered intracellular localization of MyoD and Id1. These results demonstrate in vivo that E12 and E47 modulate both MyoD and Id1 degradation and may have implications for the physiological regulation of muscle development.

Effects of smoking and marination on the sensory characteristics of cold-cut chicken breast filets: A pilot study.

This study aimed to determine individual and combined effects of smoking and marination on the sensory characteristics of boneless, skinless chicken breast meat. Four types of cooked, cold-cut chicken breast meat, i.e., marinated cooked, marinated smoked, and controls of non-marinated cooked and non-marinated smoked chicken, were evaluated for 28 sensory characteristics. Marination significantly increased saltiness, sweetness, roasted flavor, smoked flavor, and moistness of the cold-cut chicken breast meat. In addition, smoking significantly enhanced the saltiness, bitterness, roasted flavor, smoked flavor, and moistness of mass. Interestingly, a combination of smoking and marination processes resulted in a synergistic increase in the perceived moistness of mass compared to their individual treatments. In conclusion, this study demonstrates individual and combined influences of smoking and marination on the sensory characteristics of cold-cut chicken breast meat.

Sweetgum: An ancient source of beneficial compounds with modern benefits.

Sweetgum trees are large, deciduous trees found in Asia and North America. Sweetgum trees are important resources for medicinal and other beneficial compounds. Many of the medicinal properties of sweetgum are derived from the resinous sap that exudes when the outer bark of the tree has been damaged. The sap, known as storax, has been used for centuries to treat common ailments such as skin problems, coughs, and ulcers. More recently, storax has proven to be a strong antimicrobial agent even against multidrug resistant bacteria such as methicillin-resistant Staphylococcus aureus. In addition to the sap, the leaves, bark, and seeds of sweetgum also possess beneficial compounds such as shikimic acid, a precursor to the production of oseltamivir phosphate, the active ingredient in Tamiflu®-an antiviral drug effective against several influenza viruses. Other extracts derived from sweetgum trees have shown potential as antioxidants, anti-inflammatory agents, and chemopreventive agents. The compounds found in the extracts derived from sweetgum sap suppress hypertension in mice. Extracts from sweetgum seeds have anticonvulsant effects, which may make them suitable in the treatment of epilepsy. In addition to the potential medicinal uses of sweetgum extracts, the extracts of the sap possess antifungal activity against various phytopathogenic fungi and have been effective treatments for reducing nematodes and the yellow mosquito, Aedes aegypti, populations thus highlighting the potential of these extracts as environment-friendly pesticides and antifungal agents. The list of value-added products derived from sweetgum trees can be increased by continued research of this abundantly occurring tree.

Temperature effects on the antimicrobial efficacy of condensed smoke and lauric arginate against Listeria and Salmonella.

Condensed smoke or liquid smoke (LS) and lauric arginate (LAE) are antimicrobials used in food preservation. They have demonstrated abilities to reduce or inhibit pathogenic and spoilage organisms. Few studies, however, have reported on the effectiveness of LS or LAE over the range of temperatures typically encountered in food marketing channels. Therefore, the effects of temperature on the antimicrobial properties of two commercial LS fractions, an LS derived from pecan shells, and LAE against two common foodborne pathogens, Listeria and Salmonella, were investigated. The MICs of the three LS samples and LAE were measured at 4, 10, and 37°C for Listeria monocytogenes strains 2045 (Scott A, serotype 4b) and 10403S (serotype 1/2a) and two strains of Listeria innocua, a well-established surrogate, and at 10, 25, and 37°C for Salmonella enterica serovar Typhimurium and Salmonella enterica serovar Heidelberg. The MICs for LS against Listeria ranged from 3 to 48% (vol/vol), with higher MICs seen with lower temperatures. The MICs for LS on Salmonella ranged from 3 to 24%. Values for LAE ranged between 0.004 and 0.07% for both pathogens, and like LS, higher MICs were always associated with lower incubation temperatures. Understanding how storage temperature affects the efficacy of antimicrobials is an important factor that can contribute to lowering the hurdles of use levels and costs of antimicrobials and ultimately improve food safety for the consumer.

Functionality of liquid smoke as an all-natural antimicrobial in food preservation.

The smoking of foods, especially meats, has been used as a preservation technique for centuries. Today, smoking methods often involve the use of wood smoke condensates, commonly known as liquid smoke. Liquid smoke is produced by condensing wood smoke created by the pyrolysis of sawdust or wood chips followed by removal of the carcinogenic polyaromatic hydrocarbons. The main products of wood pyrolysis are phenols, carbonyls and organic acids which are responsible for the flavor, color and antimicrobial properties of liquid smoke. Several common food-borne pathogens such as Listeria monocytogenes, Salmonella, pathogenic Escherichia coli and Staphylococcus have shown sensitivity to liquid smoke in vitro and in food systems. Therefore liquid smoke has potential for use as an all-natural antimicrobial in commercial applications where smoke flavor is desired. This review will cover the application and effectiveness of liquid smoke and fractions of liquid smoke as an all-natural food preservative. This review will be valuable for the industrial and research communities in the food science and technology areas.

Determinants of nuclear and cytoplasmic ubiquitin-mediated degradation of MyoD.

The ubiquitin-proteasome system is responsible for the regulation and turnover of many short-lived proteins both in the cytoplasm and in the nucleus. Degradation can occur via two distinct pathways, an N terminus-dependent pathway and a lysine-dependent pathway. The pathways are characterized by the site of initial ubiquitination of the protein, the N terminus or an internal lysine, respectively. MyoD, a basic helix-loop-helix transcription factor, is a substrate for the ubiquitin-proteasome pathway and is degraded in the nucleus. It is preferentially tagged for degradation on the N terminus and thus is degraded by the N terminus-dependent pathway. Addition of a 6x Myc tag to the N terminus of MyoD can force degradation through the lysine-dependent pathway by preventing ubiquitination at the N-terminal site. Modifications of the nuclear localization signal and nuclear export signal of MyoD restrict ubiquitination and degradation to the cytoplasm or the nucleus. Using these mutants, we determined which degradation pathway is dominant in the cytoplasm and the nucleus. Our results suggest that the lysine-dependent pathway is the more active pathway within the cytoplasm, whereas in the nucleus the two pathways are both active in protein degradation.