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Xin Liu,Xin-Huai Zhao 한국식품과학회 2017 Food Science and Biotechnology Vol.26 No.3
Mucor-fermented Mao-tofu at 3–7 days was extracted using water (pH 4.5 and pH 6.5) and ethanol solutions (40 and 80%, v/v). At protein concentration of 40 lg/mL, all the extracts showed immune activities via activating macrophages, splenocytes, and natural killer cells, which enhances the secretion of interleukin (IL)-2, interferon-c, tumor necrosis factor-a, IL-1b, IL-6, inducible nitric oxide synthase, and lysozyme, but inhibits the secretion of IL-4. All the extracts exhibited higher activities than that of soybean protein, demonstrating that Mucor-mediated fermentation enhanced the immune potentials of Mao-tofu. Fermentation time of 6 days ensured the extracts the highest activities, whereas lower activities were detected. The highest and lowest activities were detected on using a solution of water (pH 6.5) and 40% ethanol, respectively. The extract obtained using water (pH 6.5) contained more Arg and Cys with immune significance, which partially contributed to its high activities. Both fermentation times and extracting solvents were thus proved to affect the immune activities of soluble Maotofu extracts.
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Chang-Yue Zhu,Xiao-Peng Wang,Xin-Huai Zhao 한국식품과학회 2015 Food Science and Biotechnology Vol.24 No.3
Transglutaminase at a concentration of 10 kU/kg of protein and degraded chitosan were used for glycosylation and crosslinking of caseinate at a fixed molar ratio of the acyl acceptor to the acyl donor of 3:1, a protein concentration of 50 g/L, a pH 7.5 at 37oC, and a reaction time of 4 h. Electrophoretic and chemical analyses showed glycosylation and crosslinking of caseinate. Glycosylated and crosslinked caseinate (GC-caseinate) contained glucosamine at 12.77 g/kg of protein, and the protein fraction had fewer reactable amino groups than original caseinate (0.58 vs. 0.64 mol/kg of protein). GC-caseinate exhibited an enhanced surface hydrophobicity, in vitro digestibility, water-binding capacity, and rheological properties, with poor protein dispensability and emulsification activity, but a similar oilbinding capacity and emulsion stability, compared with original caseinate. GC-caseinate also exhibited better properties than transglutaminase-crosslinked caseinate. Glycosylation and crosslinking was effective for better water-binding and rheological properties of caseinate.
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