메뉴 건너뛰기




Volumn 43, Issue 5, 2008, Pages 480-487

Enzymatic production of bioactive peptides from sericin recovered from silk industry wastewater

Author keywords

Antioxidant; Bioactive peptide; Hydrolysate; Response surface methodology; Sericin; Tyrosinase

Indexed keywords

BIOACTIVITY; HYDROLYSIS; MOISTURE; PEPTIDES;

EID: 41549119752     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2007.11.018     Document Type: Article
Times cited : (72)

References (25)
  • 1
    • 0034264573 scopus 로고    scopus 로고
    • Silk protein, sericin, suppresses colon carcinogenesis induced by 1,2-dimethylhydrazine in mice
    • Sasaki M., Kato N., Watanabe H., and Yamada H. Silk protein, sericin, suppresses colon carcinogenesis induced by 1,2-dimethylhydrazine in mice. Oncol Rep 7 (2000) 1049-1052
    • (2000) Oncol Rep , vol.7 , pp. 1049-1052
    • Sasaki, M.1    Kato, N.2    Watanabe, H.3    Yamada, H.4
  • 2
    • 0036268771 scopus 로고    scopus 로고
    • Applications of natural silk protein sericin in biomaterials
    • Zhang Y.Q. Applications of natural silk protein sericin in biomaterials. Biotechnol Adv 20 (2002) 91-100
    • (2002) Biotechnol Adv , vol.20 , pp. 91-100
    • Zhang, Y.Q.1
  • 3
    • 0030153195 scopus 로고    scopus 로고
    • Treatment of wastewater from silk degumming processes for protein recovery and water reuse
    • Fabiani C., Pizzichini M., Spadoni M., and Zeddita G. Treatment of wastewater from silk degumming processes for protein recovery and water reuse. Desalination 105 (1996) 1-9
    • (1996) Desalination , vol.105 , pp. 1-9
    • Fabiani, C.1    Pizzichini, M.2    Spadoni, M.3    Zeddita, G.4
  • 4
    • 15944391324 scopus 로고    scopus 로고
    • Preparation and structure of porous silk sericin materials
    • Wei T., Li M.Z., and Xie R.J. Preparation and structure of porous silk sericin materials. Macromol Mater Eng 290 (2005) 188-194
    • (2005) Macromol Mater Eng , vol.290 , pp. 188-194
    • Wei, T.1    Li, M.Z.2    Xie, R.J.3
  • 6
    • 41549119075 scopus 로고    scopus 로고
    • Tamada Y. Anticoagulant and its production. Japan Patent. JP 09-227402A; 1997.
    • Tamada Y. Anticoagulant and its production. Japan Patent. JP 09-227402A; 1997.
  • 7
    • 0035489909 scopus 로고    scopus 로고
    • Supplemental silk protein, sericin, suppresses colon tumorigenesis in 1,2-dimethylhydrazine-treated mice by reducing oxidative stress and cell proliferation
    • Zhaorigetu S., Sasaki M., Watanabe H., and Kato N. Supplemental silk protein, sericin, suppresses colon tumorigenesis in 1,2-dimethylhydrazine-treated mice by reducing oxidative stress and cell proliferation. Biosci Biotechnol Biochem 65 (2001) 2181-2186
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 2181-2186
    • Zhaorigetu, S.1    Sasaki, M.2    Watanabe, H.3    Kato, N.4
  • 8
    • 0034950803 scopus 로고    scopus 로고
    • Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin
    • Tsujimoto K., Takagi H., Takahashi M., Yamada H., and Nakamori S. Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin. J Biochem 129 (2001) 979-986
    • (2001) J Biochem , vol.129 , pp. 979-986
    • Tsujimoto, K.1    Takagi, H.2    Takahashi, M.3    Yamada, H.4    Nakamori, S.5
  • 9
    • 0033807237 scopus 로고    scopus 로고
    • Consumption of silk protein, sericin elevates intestinal absorption of zinc, iron, magnesium and calcium in rats
    • 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 (2000) 1505-1511
    • (2000) Nutr Res , vol.20 , pp. 1505-1511
    • Sasaki, M.1    Yamada, H.2    Kato, N.3
  • 10
    • 0008779196 scopus 로고    scopus 로고
    • A resistant protein, sericin improves atropine-induced constipation in rats
    • Sasaki M., Yamada H., and Kato N. A resistant protein, sericin improves atropine-induced constipation in rats. Food Sci Technol Res 6 (2000) 280-290
    • (2000) Food Sci Technol Res , vol.6 , pp. 280-290
    • Sasaki, M.1    Yamada, H.2    Kato, N.3
  • 11
    • 0004878601 scopus 로고    scopus 로고
    • Physiological functions of buck wheat protein and sericin as resistant proteins
    • Kato N., Kayashita J., and Sasaki M. Physiological functions of buck wheat protein and sericin as resistant proteins. J Jap Soc Nutr Food Sci 53 (2000) 71-75
    • (2000) J Jap Soc Nutr Food Sci , vol.53 , pp. 71-75
    • Kato, N.1    Kayashita, J.2    Sasaki, M.3
  • 12
    • 0025482614 scopus 로고
    • Intestinal absorption of protein hydrolysis products: a review
    • Webb K.E. Intestinal absorption of protein hydrolysis products: a review. J Anim Sci 68 (1990) 3011-3022
    • (1990) J Anim Sci , vol.68 , pp. 3011-3022
    • Webb, K.E.1
  • 13
    • 0034101865 scopus 로고    scopus 로고
    • Isolation and characterization of free radical scavenging activities peptides derived from casein
    • Suetsuna K., Ukeda H., and Ochi H. Isolation and characterization of free radical scavenging activities peptides derived from casein. J Nutr Biochem 11 (2000) 128-131
    • (2000) J Nutr Biochem , vol.11 , pp. 128-131
    • Suetsuna, K.1    Ukeda, H.2    Ochi, H.3
  • 14
    • 33751154733 scopus 로고
    • Structural analysis of antioxidative peptides from soybean
    • Chen H.M., Muramoto K., and Yamauchi F. Structural analysis of antioxidative peptides from soybean. J Agric Food Chem 43 (1995) 574-578
    • (1995) J Agric Food Chem , vol.43 , pp. 574-578
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3
  • 15
    • 33947495452 scopus 로고    scopus 로고
    • Preparation and characterization of sericin powder extracted from silk industry wastewater
    • Wu J.H., Zhang W., and Xu S.Y. Preparation and characterization of sericin powder extracted from silk industry wastewater. Food Chem 103 (2007) 1255-1262
    • (2007) Food Chem , vol.103 , pp. 1255-1262
    • Wu, J.H.1    Zhang, W.2    Xu, S.Y.3
  • 18
    • 0004202155 scopus 로고
    • Association of Official Analytical Chemists, Washington, DC
    • AOAC. Official Methods Of Analysis. 15th ed. (1990), Association of Official Analytical Chemists, Washington, DC
    • (1990) Official Methods Of Analysis. 15th ed.
    • AOAC1
  • 19
    • 0001343757 scopus 로고
    • Role of ferritin as a lipid oxidation catalyst in muscle food
    • Deker E.A., and Welc B. Role of ferritin as a lipid oxidation catalyst in muscle food. J Agric Food Chem 38 (1990) 674-677
    • (1990) J Agric Food Chem , vol.38 , pp. 674-677
    • Deker, E.A.1    Welc, B.2
  • 20
    • 0000209774 scopus 로고
    • Studies on products of browning reactions: antioxidative activities of products of browning reaction prepared from glucosamine
    • Oyaizu M. Studies on products of browning reactions: antioxidative activities of products of browning reaction prepared from glucosamine. Jpn J Nutr 44 (1986) 307-315
    • (1986) Jpn J Nutr , vol.44 , pp. 307-315
    • Oyaizu, M.1
  • 21
    • 0032562101 scopus 로고    scopus 로고
    • Oxyresveratrol as the potent inhibitor on dopa oxidase activity of mushroom tyrosinase
    • Shin N.H., Ryu S.Y., Choi E.J., Kang S.H., Chang I.M., Min K.R., et al. Oxyresveratrol as the potent inhibitor on dopa oxidase activity of mushroom tyrosinase. Biochem Biophys Res Commun 243 (1998) 801-803
    • (1998) Biochem Biophys Res Commun , vol.243 , pp. 801-803
    • Shin, N.H.1    Ryu, S.Y.2    Choi, E.J.3    Kang, S.H.4    Chang, I.M.5    Min, K.R.6
  • 22
    • 15344342219 scopus 로고    scopus 로고
    • Antioxidative properties and stability of ethanolic extracts of holy basil and Galangal
    • Juntachote T., and Berghofer E. Antioxidative properties and stability of ethanolic extracts of holy basil and Galangal. Food Chem 92 (2005) 193-202
    • (2005) Food Chem , vol.92 , pp. 193-202
    • Juntachote, T.1    Berghofer, E.2
  • 23
    • 0142092755 scopus 로고    scopus 로고
    • Inhibitory effects of cupferron on the monophenolase and diphenolase activity of mushroom tyrosinase
    • Xie L.P., Chen Q.X., Huang H., Liu X.D., Chen H.T., and Zhang R.Q. Inhibitory effects of cupferron on the monophenolase and diphenolase activity of mushroom tyrosinase. Int J Biochem Cell Biol 35 (2003) 1658-1666
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 1658-1666
    • Xie, L.P.1    Chen, Q.X.2    Huang, H.3    Liu, X.D.4    Chen, H.T.5    Zhang, R.Q.6
  • 24
    • 0027504187 scopus 로고
    • Dietary antioxidant flavonoids and risk of coronary heart disease: the Zutphen elderly study
    • Hertog M.G., Fesrens E.J., Hollman P.C., Katan M.B., and Kromhout D. Dietary antioxidant flavonoids and risk of coronary heart disease: the Zutphen elderly study. Lancet 342 (1993) 1007-1011
    • (1993) Lancet , vol.342 , pp. 1007-1011
    • Hertog, M.G.1    Fesrens, E.J.2    Hollman, P.C.3    Katan, M.B.4    Kromhout, D.5
  • 25
    • 0002129872 scopus 로고    scopus 로고
    • Antioxidants and cancer: the epidemiological evidence
    • Garewal H.S. (Ed), CRC Press, Boca Raton
    • McLarty J.W. Antioxidants and cancer: the epidemiological evidence. In: Garewal H.S. (Ed). Antioxidants and Disease Prevention (1997), CRC Press, Boca Raton 45-65
    • (1997) Antioxidants and Disease Prevention , pp. 45-65
    • McLarty, J.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.