• Title/Summary/Keyword: Tyrosinase activity

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A Study on the Stability and Moisturizing Effect for the Cream Containing Castanea crenata Leaf Extract (밤나무 잎 추출물 함유 크림의 안정성 및 피부 보습효과에 관한 연구 (2))

  • Kim, Jin-Young;Park, Soo-Nam
    • Journal of the Society of Cosmetic Scientists of Korea
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    • v.35 no.4
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    • pp.301-307
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    • 2009
  • In the previous study, we evaluated and reported about the anti-oxidative activities of extract/fraction of Castanea crenata leaf. Extract/fraction of Castanea crenata leaf showed excellent free radical scavenging activity, cell protective activity and inhibitory activity on tyrosinase and elastase. In this study, in order to investigate the stability of cream containing 0.2 % Castanea crenata ethyl acetate fraction. pH, viscosity, and absorbance were measured under 4 different temperature ($4^{\circ}C$, $20^{\circ}C$, $37^{\circ}C$, $45^{\circ}C)$ and under the sun light at 2 weeks intervals for the 8 weeks. The variations on pH and viscosity of all experimental creams were similar to control cream. The absorbance variation of extract from experimental cream at 353 nm was in the order: under the sun > $45^{\circ}C$ > $37^{\circ}C$ > $20^{\circ}C$ > $4^{\circ}C$. It shows that ethyl acetate fraction in the cream can be oxidized under the sun. The bad smell and discoloration were not shown. Also, physical changes as creaming and cohesion were not shown. Also, transepidermal water loss (TEWL) and water contents in skin were measured. The cream containing Castanea cranata leaf extract was applied to the right lower arm. After 120 min, TEWL of parts was decreased as 29.7 % (experimental cream) and 5.4 % (control cream) respectively. And the water contents in skin were increased 22.6 % (experimental cream) and 24.7 % (control cream) respectively. It was confirmed that a cream containing ethyl acetate fraction of Castanea crenata leaf shows the superior moisturizing effect. The results showed that Castanea crenata leaf extract could be used as a new active ingredient for anti-aging cosmeceuticals.

The Biological Activity from Prunella vulgaris Extracts (하고초(Prunella vulgaris) 추출물의 생리활성)

  • Kim, Jin-Sung;Lee, Ju-Yeong;Park, Ki-Tae;An, Bong-Jeun;Lee, Sun-Ho;Cho, Young-Je
    • Food Science and Preservation
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    • v.20 no.2
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    • pp.234-241
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    • 2013
  • The phenolic compounds of water extracts from Prunella vulgaris were highest at 9.25 mg/g, respectively, when various extraction solvents were used. The optimum condition for extracting phenolic compounds from Prunella vulgaris was extraction in water for 18hr. The DPPH-scavenging activities of Prunella vulgaris were highest at the water extracts. The ABTS radical cation decolorization was higher than 40% in the range of 0~100% ethanol extract section. The antioxidant protection factor on the lipophilic phenolic metabolites was shown to be 1.1 PF in the water extracts from Prunella vulgaris. The TBARS was lower than the control ($0.53{\mu}M$) in all the sections. The tyrosinase inhibitory effect, which is related to skin whitening, was above 40%, and for the anti-wrinkle effect, the elastase inhibition activity was above 40% at 0.2 mg/mL. The astringent effect of the Prunella vulgaris 40% ethanol extracts was 98.1% at 1 mg/mL. As a result, it can be concluded that Prunella vulgaris has the potential to be used as a cosmetic material.

Endogenous Phenoloxidase Purified from an Earthworm, Lumbricus rubellus (붉은 지렁이(Lumbricus rubellus) 체내로부터 정제한 Phenoloxidase)

  • 백승렬;조은정;유경희;김유삼;서정진;장정순
    • The Korean Journal of Zoology
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    • v.39 no.1
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    • pp.36-46
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    • 1996
  • An endogenous phenoloxidase (EPO) from earthworm, Lumbricus rubellus, has been purified and characterized. The purified EPO using ammonium sulfate fractionation, Blue-2, Phenyl-, and Q-sepharose chromatography steps was revealed in SDS-PAGE as a single protein banri with Mr. of 59 kl)a. A native strudure of the enzyme was examined with an in situ staining of a nondenatudng-PAGE using DL-dopa as a substrate. The result showed that a single band due to the EPO activity was located siighdy above a standard polypeptide with Mr. of 210 kl)a. These fads indicate that the EPO is an oligomeric enzyme. The presence of a monophenolase activity of the purified EPO, which hydroxylates tyrosine to dopa, was confirmed by observing dopachrome accumulation at 475 nm at PH 8.0 with a typical lag phase during 60 mm. of meausrement. A series of inhibition study has been performed for the enzyme with several divalent cation chelators such as phenyithiourea (Flu), 1, lO-phenanthroline, EDTA, and EGTA. Among them, only V'flj inhibited the enzyme with 1C0.5 of 65 MM, which indicated that copper was critical for the catalysis of EPO. The enzyme was maximally active at 35'C and pH 8.0 when L-dopa to dopachrome conversion was spectrophotometricaily monitored at 475 nm. The apparent Km values of P0 for L-opa were obtained as 1.86 mM and 13.8 mM at pH 6.5 and 8.0, respectively. The catalytic efficiencies at both pH were almost identical [(kat/Km)pH8.0/(kcat/Km)pH6.5 = O.92] while the Vmax at p11 8.0 was 6.6-fold higher than that at pH 6.5. This fact may indicate that pH affeds the catalysis at substrate and/or enzyme-substrate complex level rather than the enzyme itself. Taken together, the EPO was an oligomeric enzyme which did not require proteolysis for its activation. These results also indicated that the enzyme can exist, at least, in part as a latent form In vivo, which might be distinct from the prophenoloxidase activating system. Therefore, it is pertinent to consider that there must be certain regulatory molecules or phenomena in L. rubellus which make the 1,0 in a latent form in vivo before the foreign invasions.

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