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자료유형
학술저널
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저널정보
한국잠사학회 International Journal of Industrial Entomology International Journal of Industrial Entomology 제9권 제1호
발행연도
2004.1
수록면
29 - 33 (5page)

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Low molecular weight silk fibroin (LMSF), which was prepared by hydrolysis of silk fibroin using hightemperature and high-pressure method, was found to inhibit the oxidation of L-3,4,-dihydroxyphenylalanine (L-DOPA) catalyzed by mushroom tyrosinase (EC 1.14.18.1). LMSF contained mostly free amino acids such as L-glycine, L-alanine, and L-serine and oligopeptides, mainly glycine-alanine dimer. As a result of analyzing the inhibition kinetics from Lineweaver- Burk plots, L-glycine and glycine-alanine dimer showed noncompetitive behavior while uncompetitive behavior was observed in L-alanine, and Lserine. When weight percent concentration of ID50 was compared, L-glycine was most effective on the inhibition and LMSF was also good enough for the inhibition effect of tyrosinase activity. LMSF showed a mixed-type inhibition and the inhibitory mechanism of LMSF might be caused by free amino acids and oligopeptides. As a result of spectroscopic observation with time, initial rate of increase of DOPAchrome decreased remarkably and the time to reach maximum absorbance increased as an increase of the concentration of L-glycine, meaning that L-glycine made itself mainly responsible for the formation of chelate with Cu2+ in tyrosinase. However, in case of Lalanine, L-serine, and especially glycine-alanine dimmer, the production of DOPAchrome after an arrival at maximum absorbance decreased, indicating the production of adducts through the reaction with DOPAquinone.

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