Interfacial behavior of fatty-acylated sericin prepared by lipase-catalyzed solid-phase synthesis

Bioscience, Biotechnology and Biochemistry

Volumn 70, Issue 1, 2006, Pages 66-75

  Ogino, Masato ^a   Tanaka, Rie ^a   Hattori, Makoto ^a   Yoshida, Tadashi ^a   Yokote, Yoshiko ^b   Takahashi, Koji ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^b JOSAI UNIVERSITY   (Japan)

Author keywords

Acylation with lipase; Emulsifying ability; Interfacial behavior; Moistness; Sericin

Indexed keywords

ACYLATION; EMULSIFICATION; HYDROPHOBICITY; MOLECULAR WEIGHT; OLEIC ACID; SYNTHESIS (CHEMICAL);

ACYLATION WITH LIPASE; EMULSIFYING ABILITY; INTERFACIAL BEHAVIOR; MOISTNESS; SERICIN;

ENZYMES;

FATTY ACID; IMMOBILIZED ENZYME; SERICIN; SODIUM CHLORIDE; TRIACYLGLYCEROL LIPASE; WATER;

ACYLATION; ANIMAL; ARTICLE; CATALYSIS; CHEMISTRY; DRUG EFFECT; EMULSION; INFRARED SPECTROSCOPY; KINETICS; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARTICLE SIZE; PH; PROTEIN SECONDARY STRUCTURE; SILKWORM; TEMPERATURE; WOOL;

ACYLATION; ANIMALS; BOMBYX; CATALYSIS; EMULSIONS; ENZYMES, IMMOBILIZED; FATTY ACIDS; HYDROGEN-ION CONCENTRATION; KINETICS; LIPASE; MAGNETIC RESONANCE SPECTROSCOPY; PARTICLE SIZE; PROTEIN STRUCTURE, SECONDARY; SERICINS; SODIUM CHLORIDE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; WATER; WOOL;

EID: 31444445322     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70.66     Document Type: Article

References (30)

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).