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Bioscience, Biotechnology, and Biochemistry Volume 70, 2006 - Issue 1
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Original Articles

Interfacial Behavior of Fatty-Acylated Sericin Prepared by Lipase-Catalyzed Solid-Phase Synthesis

Masato OGINODepartment of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
,
Rie TANAKADepartment of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
,
Makoto HATTORIDepartment of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
,
Tadashi YOSHIDADepartment of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
,
Yoshiko YOKOTEDepartment of Chemistry, Faculty of Science, Josai University
&
Koji TAKAHASHIDepartment of Applied Biological Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology
Pages 66-75 | Received 18 May 2005, Accepted 05 Sep 2005, Published online: 22 May 2014

  • 1) Fournier, A., Quantitative data on the Bombyx mori L. silk worm. Biochimie, 61, 283–320 (1979).
  • 2) Kato, N., Sato, S., Yamanaka, A., Yamada, H., Fuwa, N., and Nomura, M., Silk protein, sericin, inhibits lipid peroxidation and tyrosinase activity. Biosci. Biotechnol. Biochem., 62, 145–147 (1998).
  • 3) Voegeli, R., Sericin silk protein: unique structure and properties. Cosmetics Toiletries, 108, 101–108 (1993).
  • 4) Tsujimoto, K., Takagi, M., Takahashi, M., Yamada, H., and Nakamori, S., Cryoprotective effect of the sericin-rich repetitive sequence in silk protein sericin. J. Biochem., 129, 979–986 (2001).
  • 5) Sasaki, M., Yamada, H., and Kato, N., A resistant protein, sericin, improves atropin-induced constipation in rats. Food Sci. Technol. Res., 6, 280–283 (2000).
  • 6) Sasaki, M., Yamada, H., and Kato, N., Consumption of silk protein, sericin, elevates intestinal absorption of zinc, iron, magnesium and calcium in rats. Nutr. Res., 20, 1505–1511 (2000).
  • 7) Zhaorigetu, S., Sakaki, M., Watanabe, H., and Kato, N., Supplemental silk protein, sericin, suppresses tumorigenesis in 1,2-dimethylhydrazine-treated mice by reducing oxidative stress and cell proliferation. Biosci. Biotechnol. Biochem., 65, 2181–2186 (2001).
  • 8) Zhang, Y.-Q., Applications of natural silk protein sericin in biomaterials. Biotechnol. Adv., 20, 91–100 (2002).
  • 9) Tamada, Y., Sano, M., Niwa, K., Imai, T., and Yoshino, G., Sulfation of silk sericin and anticoagulant activity of sulfated sericin. J. Biomat. Sci. Polym. Ed., 15, 971–980 (2004).
  • 10) Haque, Z., Matoba, T., and Kito, M., Incorporation of fatty acid into food protein: palmitoyl soybean glycinin. J. Agric. Food Chem., 30, 481–486 (1982).
  • 11) Haque, Z., and Kito, M., Lipophilization of α-S1-casein. 1. Covalent attachment of palmitoyl residue. J. Agric. Food Chem., 31, 1225–1230 (1983).
  • 12) Ibrahim, H. R., Kato, A., and Kobayashi, K., Antimicrobial effects of lysozyme against gram-negative bacteria due to covalent binding of palmitic acid. J. Agric. Food Chem., 30, 2077–2082 (1991).
  • 13) Ibrahim, H. R., Kobayashi, K., and Kato, A., Length of hydrocarbon chain and antimicrobial action to gram-negative bacteria of fatty acylated lysozyme. J. Agric. Food Chem., 41, 1164–1168 (1993).
  • 14) Takahashi, K., Lou, X.-F., Ishii, Y., and Hattori, M., Lysozyme-glucose stearic acid monoester conjugate formed through the Maillard reaction as an antibacterial emulsifier. J. Agric. Food Chem., 48, 2044–2049 (2000).
  • 15) Kobata, K., Kawaguchi, M., and Watanabe, T., Enzymatic synthesis of a capsinoid by acylation of vanillyl alcohol with fatty acid derivatives catalyzed by lipase. Biosci. Biotechnol. Biochem., 66, 319–327 (2002).
  • 16) Bradoo, S., Saxena, R. K., and Gupta, R., High yields of ascorbyl palmitate by thermostable lipase-mediated esterification. J. Am. Oil Chem. Soc., 76, 1291–1295 (1999).
  • 17) Pereira, C. C., de Silva, M. A., and Langone, M. A., Enzymatic synthesis of monolaurin. Appl. Biochem. Biotechnol., Spring, 113–116, 433–445 (2004).
  • 18) Larios, A., Garcia, H. S., Oliart, R. M., and Valerio-Alfaro, G., Synthesis of flavor and fragrance esters using Candida antratica lipase. Appl. Microbiol. Biotechnol., 65, 373–376 (2004).
  • 19) Cao, L., Bornscheuer, U. T., and Schmid, R. D., Lipase-catalyzed solid phase synthesis of sugar esters. Biocatal. Biotransform., 14, 269–283 (1997).
  • 20) Takahashi, K., Yamamoto, H., Yokote, Y., and Hattori, M., Thermal behavior of fowl feather keratin. Biosci. Biotechnol. Biochem., 68, 1875–1881 (2004).
  • 21) Dong, A., Hung, P., and Caughey, W. S., Protein secondary structure in water from secondary-derivative amide I infrared spectra. Biochem., 29, 3303–3308 (1990).
  • 22) Beer, M., Sutherland, G. B. B. M., Tanner, K. N., and Wood, D. L., Infrared spectra an structure of protein. Proc. Roy. Soc., 249, 147–172 (1959).
  • 23) Komatsu, K., Chemical and structural studies on silk sericin. Proc. 7th Int. Wool Text. Res. Conf., 1, 372–382 (1985).
  • 24) Lee, K., Kweon, H., Woo, S.-O., Lee, Y.-W., Kim, K.-H., and Park, Y.-H., Effect of methyl alcohol on the morphology and conformational characteristics of silk sericin. Int. J. Biol. Macromol., 33, 75–80 (2003).
  • 25) Pearce, K. M., and Kinsella, J. E., Emulsifying properties of proteins: evaluation of a turbidimetric technique. J. Agric. Food Chem., 26, 716–723 (1978).
  • 26) Itzaki, R. F., and Gill, D. M., A micro-biuret method for estimating proteins. Anal. Biochem., 9, 401–410 (1964).
  • 27) Hattori, M., and Takahashi, K., Pepsin-solubilized elastin as a water/oil emulsifier. Food Hydrocolloids, 7, 327–335 (1993).
  • 28) Nakazaki, S., Takaku, K., Yuguchi, M., Edamatsu, H., and Takahashi, K., Regulation of molecular structure of acid-dispersed collagen with alkaline pretreatment. Animal Sci. Technol., 65, 1018–1025 (1994).
  • 29) Yamagishi, Y., Hattori, M., Yoshida, T., and Takahashi, K., Improvement of the functional properties of sucrose stearate by phosphorylation. J. Agric. Food Chem., 52, 8039–8045 (2004).
  • 30) Nagasawa, K., Takahashi, K., and Hattori, M., Improved emulsifying properties of β-lactoglobulin by conjugating with carboxymethyl dextran. Food Hydrocolloids, 10, 63–67 (1996).

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