References
- K. Sprague, The Bombyx mori silk proteins: characterization of large polypeptides, Biochemistry, 14(5), 925 (1975) https://doi.org/10.1021/bi00676a008
- T. Gamo, T. Inokuchi, and H. Laufer, Polypeptides of fibroin and sericin secreted from the different sections of the silk gland in Bombyx mori, Insect Biochem., 7(3), 285 (1977) https://doi.org/10.1016/0020-1790(77)90026-9
- Y. Takasu, H. Yamada, and K. Tsubouchi, Isolation of three main sericin components from the cocoon of the silkworm, Bombyx mori, Biosci. Biotech. Bioch., 66(12), 2715 (2002) https://doi.org/10.1271/bbb.66.2715
- K. Kato, S. Sato, A. Yamanaka, H. Yamada, N. Fuwa, and M. Nomura, Silk protein, sericin, inhibits lipid peroxidation and tyrosinase activity, Biosci. Biotechnol. Biochem., 62(1), 145 (1998) https://doi.org/10.1271/bbb.62.145
- S. Zhaorigetu, N. Yanaka, M. Sasaki, H. Watanabe, and N. Kato, Inhibitory effects of silk protein, sericin on UVB-induced acute damage and tumor promotion by reducing oxidative stress in the skin of hairless mouse, J. Photochem. Photobiol. B: Biol., 71(1-3), 11 (2003) https://doi.org/10.1016/S1011-1344(03)00092-7
- M. Sasaki, H. Yamada, and N. Kato, Consumption of silk protein, sericin elevates intestinal absorption of zinc, iron, magnesium and calcium in rats, Nutr. Res., 20(9), 1505 (2000) https://doi.org/10.1016/S0271-5317(00)80031-7
- S. Zhaorigetu, M. Sasaki, H. Watanabe, and N. Kato, Supplemental silk protein, sericin, suppresses colon tumorigenesis in 1,2-dimethylhydrazine-treated mice by reducing oxidative stress and cell proliferation, Biosci. Biotechnol. Biochem., 65(10), 2181 (2001) https://doi.org/10.1271/bbb.65.2181
- K. Tsujimoto, H. Takagi, M. Takahashi, H. Yamada, and S. Nakamori, Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin, J. Biochem., 129(6), 979 (2001) https://doi.org/10.1093/oxfordjournals.jbchem.a002946
- M. Takahashi, K. Tsujimoto, H. Yamada, H. Takagi, and S. Nakamori, The silk protein, sericin, protects against cell death caused by acute serum deprivation in insect cell culture, Biotechnol. Lett., 25(21), 1805 (2003) https://doi.org/10.1023/A:1026284620236
- J. H. Kim and D. G. Bae, Hydrolysis characteristics and application of silk sericin; II. Characteristics of soluble sericin and its application on human skin, Korean J. Seric. Sci., 45(1), 58 (2003)
- J. H. Wu, Z. Wang, and S. Y. Xu, Enzymatic production of bioactive peptides from sericin recovered from silk industry wastewater, Process Biochemistry, 43(5), 480 (2008) https://doi.org/10.1016/j.procbio.2007.11.018
- R. J. Beynon, Proteolytic enzymes : a practical approach, eds. J. S. Bond, 38, Oxford University Press, England (1989)
- S. Sindayikengera and W. Xia, Nutritional evaluation of caseins and whey proteins and their hydrolysates from protamex, J. Zhejiang Univ. Sci. B, 7(2), 90 (2006) https://doi.org/10.1631/jzus.2006.B0090
- R. Marcuss, Antioxidative effect of amino acids, Nature, 186, 886 (1960) https://doi.org/10.1038/186886a0
- A. Anghileri, R. Lantto, K. Kruus, C. Arosio, and G. Freddi, Tyrosinase-catalyzed grafting of sericin peptides onto chitosan and production of protein-polysaccharide bioconjugates, J. Biotechnol., 127(3), 508 (2007) https://doi.org/10.1016/j.jbiotec.2006.07.021
- G. D. Kang, K. H. Lee, C. S. Ki, and Y. H. Park, Crosslinking reaction of phenolic side chains in silk fibroin by tyrosinase, Fiber. Polym., 5(3), 234 (2004) https://doi.org/10.1007/BF02903006