Treats are offered to dogs to reinforce the animal-owner bond and as rewards. Wheat, which contains gluten (gliadin and glutenin proteins), is often used in treats. The United States is a leading producer of sorghum which might be an alternative; however, it does not have functional properties to form viscoelastic doughs, because it is mainly composed of kafirin protein. Therefore, the objectives of this study were to determine the effects of supplementing soluble animal proteins in whole sorghum rotary-molded baked dog treats on dog preference, sensory attributes, and oxidation rate. The treats were produced in triplicate in a 2 x 4 + 1 augmented factorial arrangement of treatments. Two whole sorghum flours (WWS and WRS), four protein sources [none (NC), spray-dried plasma (SDP), egg protein (EP), and gelatin (GL)], and a positive control with wheat (WWF-GTN) were evaluated. A preference ranking test with twelve dogs was performed. Additionally, five trained panelists scored the intensity of appearance, aroma, flavor, texture/mouthfeel, and aftertaste attributes. Finally, the treats were stored at 30 °C and 60% RH, and hexanal concentrations were measured on days 0, 28, 56, and 112. The data was analyzed using the statistical software SAS for the animal and oxidation rate evaluations with significance considered at P<0.05. The descriptive sensory evaluation data was analyzed using multivariate analysis (XLSTAT). The dogs did not detect differences among WWF-GTN, WWS, or WRS treats when evaluated together. However, the WWF-GTN, WWS-SDP, and WWS-EP treatments were preferred among the white sorghum treatments. The EP treatments led to some consumption difficulties by dogs because of their hard texture. The panelists reported a high degree of variation in the appearance and texture across treatments. The WRS and WWS treats with SDP or EP were darker, while NC treats had more surface cracks. Initial crispness, hardness, and fracturability were higher in EP treatments compared to all other sorghum treatments. The predominant flavor and aftertaste identified were "grainy." The hexanal values for all treats were <1.0 mg/kg except for the EP treatments that had higher values (2.0-19.3 mg/kg) across the shelf-life test. This work indicated that the replacement of WWF-GTN by WWS and WRS, along with soluble animal proteins like SDP or GL would produce comparable preference by dogs, oxidation rates, product aromatics, flavor, aftertaste attributes, and, at a lower degree, product texture.
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http://dx.doi.org/10.1093/jas/skac191 | DOI Listing |
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Plant Breeding and Genetics Division, Nuclear Institute for Agriculture and Biology (NIAB), Faisalabad, Pakistan.
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Engine Testing Laboratory, Department of Automobile Engineering, College of Engineering and Technology, SRM Institute of Science and Technology, Kattankulathur, 603203, Tamil Nadu, India.
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School of Environment and Natural Resources, Zhejiang University of Science and Technology, Hangzhou 310023, China.
This study developed the multifunctional cellulose nanofibers (CNFs) as emulsifier for preparation of antibacterial, ultrastable and non-toxic emulsion. To achieve these properties, CNFs were oxidated using sodium periodate to introduce aldehyde groups, which served as Schiff-base reaction sites for amino groups of polyhexamethylene guanidine (PHMG), yielding PHMG-grafted CNFs (PCNFs). The modified CNFs retained good emulsification ability while acquiring antibacterial properties.
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College of Traditional Chinese Medicinal Materials, Jilin Agricultural University, Changchun 130118, China. Electronic address:
The toxicity of jellyfish Rhopilema esculentum (R. esculentum), an edible jellyfish that releases venom, has been controversial. The aim of this comprehensive study was to investigate the toxic effects of jellyfish tentacle extract (TE), which was evaluated in vivo and in vitro using ICR mice and RAW264.
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College of Veterinary Medicine, Anhui Agricultural University, 130 West Changjiang Road, Hefei, Anhui 230036, China. Electronic address:
Chicken surfactant protein A1 (cSP-A1) is a soluble C-type lectin found primarily in chicken lungs. Its function and other potential bioactivities are unclear. This study aimed to express, purify, and identify recombinant cSP-A1 (RcSP-A1), investigate its effects on chicken macrophage HD11 cells, and evaluate its ability to regulate the LPS-induced inflammatory response.
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