• Title/Summary/Keyword: tyrosinase inhibitor

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Optimal Culture Conditions on the Tyrosinase Inhibitor Production by Actinomycetes F-97 (방선균 F-97에 의한 Tyrosinase 저해제 생성 최적 배양 조건)

  • Bang, Byung-Ho;Rhee, Moon-Soo;Kim, Jin-O;Yi, Dong-Heui
    • Journal of Life Science
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    • v.17 no.6 s.86
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    • pp.798-804
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    • 2007
  • A Actinomycetes F-97 producing tyrosinase inhibitor was isolated from soil samples. The optimum culture condition for 쇼rosinase inhibitor production was investigated and the results were as follows. The best carbon source for tyrosinase inhibitor production was shown as soluble starch, the optimum concentration was 3.0%. The best nitrogen source for tyrosinase inhibitor production was shown as peptone, the optimum concentration was 0.36%. As effect of metal ions on the production of tyrosinase inhibitor, K$_2$HPO$_4$ was shown the best and the optimum concentration was 0.1 mM. The optimum pH and temperature was shown 7.0 and 30${\circ}$C, respectively. And the highest tyrosinase inhibitor production was observed at 70hr cultivation under optimum conditions in jar fermentor scale.

Syntheses of Resveratrol and its Hydroxylated Derivatives as Radical Scavenger and Tyrosinase Inhibitor

  • Lee, Hyun-Suck;Lee, Byung-Won;Kim, Mi-Ran;Jun, Jong-Gab
    • Bulletin of the Korean Chemical Society
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    • v.31 no.4
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    • pp.971-975
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    • 2010
  • Eight hydroxylated stilbene derivatives including resveratrol, desoxyrhapontigenin and piceatannol as potential radical scavenger and tyrosinase inhibitor are synthesized using optimized Wittig-Horner reaction for excellent trans-selectivity in good yields. Antioxidant activity was tested against ABTS radical and tyrosinase inhibitory activity was performed with L-tyrosine as the substrate based on previous procedure with some modification. In general, catecholic stilbenes showed stronger activity against ABTS radical and resorcinolic moiety showed stronger tyrosinase inhibitory activity. Synthetic piceatannol which containing both catecholic and resorcinolic moieties showed the strongest activity in both as ABTS radical scavenger and tyrosinase inhibitor with $IC_{50}$ values of 4.1 and $8.6\;{\mu}M$, respectively.

Production of Intracelluar Tyrosinase Inhibitor from Malassezia pachydermatis (Malassezia pachydermatis에 의한 세포 내 Tyrosinase 저해제의 생산)

  • Lee, Sung-Hyun;Yu, Hyung-Eun;Kwak, Yoon-Jin;Kim, Hyo-Jin;Lee, Dae-Hyoung;Lee, Jong-Soo
    • The Journal of Natural Sciences
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    • v.14 no.2
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    • pp.93-102
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    • 2004
  • A yeast strain SL-27 found to produce active intracellular tyrosinase inhibitor was screened from 972 kinds of yeasts. It was identified as Malassezia pachydermatis based on microbiological characteristics. The optimum pH and temperature for the growth of Malassezia pachydermatis SL-27 were pH 7.0 and $37^{\circ}C$, respectively. The optimal culture conditions for the production of tyrosinase inhibitor by Malassezia pachydermatis SL-27 were investigated. The optimal medium cimposition for tyrosinase inhibitor production was determined to be 1.0% casamino acid, 2.0% glucose, 0.1% $KH_2PO_4$, 0.05% $MgSo_{4-}7H20$ and each 0.01 of $CaCl_2$ and NaCl. Optimal initial pH and temperature for the production of tyrosinase inhibitor were pH 5.0 and $30^{\circ}C$, respectively. The maximum tyrosinase inhibitory activity of 84%/mL of cell-free extract was showed after 12 h of cultivation under the optimal culturing conditions.

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Production of Tyrosinase Inhibitor from Saccharomyces cerevisiae (Saccharomyces cerevisiae 로부터 Tyrosinase Inhibitor 의 생산)

  • Jang, In-Taek;Kim, Young-Hun;Kang, Min-Gu;Yi, Sung-Hun;Lim, Sung-Il;Lee, Jong-Soo
    • The Korean Journal of Mycology
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    • v.40 no.1
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    • pp.60-64
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    • 2012
  • Physiological functionalities of culture concentrates from various fungi were investigated. The culture concentrates from Saccharomyces cerevisiae Y277-3 showed the highest tyrosinase inhibitory activity of 42.7%. Among mold physiological functionalities, the culture concentrates from Aspergillus orygae CN20-3-1-4 showed the highest antioxidant activity of 15.8%. The other functionalities of fungi were very low or not detected. The intracellular tyrosinase inhibitor from Saccharomyces cerevisiae Y277-3, which showed the highest physiological functionalities was maximally produced when the strain was cultured in PD broth at $30^{\circ}C$ for 24 h.

Isolation and Identification of Actinomycetes F-97 Producing Tyrosinase Inhibitor (Tyrosinase 저해제를 생성하는 방선균 F-97의 분리 및 동정)

  • Bang, Byung-Ho;Rhee, Moon-Soo;Kim, Gwan-Pil;Kim, Jin-O;Yi, Dong-Heui
    • The Korean Journal of Food And Nutrition
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    • v.22 no.1
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    • pp.97-102
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    • 2009
  • In order to obtain a non-toxic and more active and stable microorganism-produced tyrosinase inhibitor, we isolated actinomycetes F-97, a producer of tyrosinase inhibitor, from soil. The aerial hyphae of this strain were gray in color with tree types. Under the microscopic examination, the isolate formed a spiral aerial spore mass with a smooth surface. The analysis of cell wall acid hydrolysate of the isolate revealed the presence of LL-diaminopimelic acid(LL-DAP). No specific sugar was detected. From these results and the cultural and physiological characteristics described in the Bergey's Manual, actinomycetes F-97 was identificated as, or best-matched to, Streptomyces aburaviensis.

Purification and Characteristics of Tyrosinase Inhibitor Produced by Actinomycetes F-97 (방선균 F-97이 생산하는 Tyrosinase 저해제의 정제 및 특징)

  • Bang, Byung-Ho;Rhee, Moon-Soo;Kim, Jin-O;Yi, Dong-Heui
    • Applied Biological Chemistry
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    • v.51 no.3
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    • pp.153-158
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    • 2008
  • An actinomycetes F-97 producing tyrosinase inhibitor was isolated from soil samples. Isolation and purification of tyrosinase inhibitor produced by F-97 was performed as follows: IRC-120 ($NH_4^+$ type) column chromatography, silica gel column chromatography, $C_{18}$ column chromatography and Sephadex LH-20 column chromatography were used successively after the centrifuged supernatant was adjusted to pH 4.0. To identify the purity of the inhibitor, octadecylsilyl(ODS) HPLC was carried out with 5% methanol as a mobile phase. Finally, the purification yield of a tyrosinase inhibitor was 5.24%. The inhibitor was very soluble in water, methanol and ethanol but insoluble in acetone, butanol, ethylacetate and chloroform. The ${\lambda}_{max}$ value of this inhibitor in water was 194nm under UV light. The biochemical test of the inhibitor was positive in Molish, Benedict, cone. $H_2SO_4$, and $KMnO_4$ tests but negative in iodine, ninhydrin, Million, Sakaguchi, xanthoproteic and Emerson tests. The tyrosinase inhibitor was stable against heat treatment of $100^{\circ}C$ for 50 minutes and pH $4{\sim}9$. The $IC_{50}$ value of this inhibitor was $19.2{\mu}g/ml$ for mushroom tyrosinase. In $1,000{\mu}g/ml$ inhibitor concentration, inhibition zone was 27 mm for Streptomyces bikiniensis NRRL B-1049. The inhibition of F-97 against mushroom tyrosinase was competitive with tyrosine.

Antioxidative Activities of Solvent Extracts from Blueberry (Blueberry 추출물의 항산화 효과)

  • Kim, Tae-Choon;Bae, Kang-Soon;Kim, Il-Kwang;Chun, Hyun-Ja
    • Journal of Physiology & Pathology in Korean Medicine
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    • v.19 no.1
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    • pp.179-183
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    • 2005
  • Recent interest in the possible protective effects of dietary antioxidant compounds against human degenerative disease has prompted investigation of foods such as blueberries, which have a high antioxidant capacity. This study was performed to determine the antioxidative activity of methanol extract and solvent fractions from blueberry. Blueberry was extracted with methanol and then fractionated with n-hexane, EtOAc, BuOH and water to get active fractions. And their antioxidant capacities in each fraction were determined by using the DPPH and FRAP assay, and tyrosinase inhibitor. Ethyl acetate fraction of blueberry exhibited antioxidant capacity.

Rosmarinic Acid as a Tyrosinase Inhibitors from Salvia miltiorrhiza

  • Kang, Hye-Sook;Kim, Hyung-Rak;Byun, Dae-Seok;Park, Hye-Jin;Choi, Jae-Sue
    • Natural Product Sciences
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    • v.10 no.2
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    • pp.80-84
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    • 2004
  • Rosmarinic acid and its methyl ester, isolated from the ethyl acetate soluble fraction of the methanolic extract of Salvia miltiorrhiza Bunge (Labiatae), were found to inhibit the oxidation of L-tyrosine catalyzed by mushroom tyrosinase with the $IC_{50}$ values of 16.8 and $21.5\;{\mu}M$, respectively. It was comparable with kojic acid, a well-known tyrosinase inhibitor, with an $IC_{50}$ of $22.4\;{\mu}M$. The inhibitory kinetics analyzed by the Lineweaver-Burk plots, were found rosmarinic acid and its methyl ester to be competitive inhibitors with $K_i\;of\;2.4{\times}10^{-5}\;and\;1.5{\times}10^{-5}\;M$, respectively.

3D-QSAR Analysis and Molecular Docking of Thiosemicarbazone Analogues as a Potent Tyrosinase Inhibitor

  • Park, Joon-Ho;Sung, Nack-Do
    • Bulletin of the Korean Chemical Society
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    • v.32 no.4
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    • pp.1241-1248
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    • 2011
  • Three dimensional quantitative structure-activity relationships (3D-QSARs) between new thiosemicarbazone analogues (1-31) as a substrate molecule and their inhibitory activity against tyrosinase as a receptor were performed and discussed quantitatively using CoMFA (comparative molecular field analysis) and CoMSIA (comparative molecular similarity indices analysis) methods. According to the optimized CoMSIA 2 model obtained from the above procedure, inhibitory activities were mainly dependent upon H-bond acceptor favored field (36.5%) of substrate molecules. The optimized CoMSIA 2 model, with the sensitivity of the perturbation and the prediction, produced by a progressive scrambling analysis was not dependent on chance correlation. From molecular docking studies, it is supposed that the inhibitory activation of the substrate molecules against tyrosinase (PDB code: 1WX2) would not take place via uncompetitive inhibition forming a chelate between copper atoms in the active site of tyrosinase and thiosemicarbazone moieties of the substrate molecules, but via competitive inhibition based on H-bonding.

버섯 배지를 이용한 tyrosinase 저해제 발효

  • Jung, Sung-Won;Han, Dae-Seok;Kim, Seok-Joong;Chun, Moon-Jin
    • Microbiology and Biotechnology Letters
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    • v.24 no.2
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    • pp.227-233
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    • 1996
  • Tyrosinase is an enzyme which catalyzes an enzymatic browning of some foods and in vivo synthesis of melanin. In order to produce natural and edible inhibitor of the enzyme which is expected to have whitening effect on melanogenesis, a microorganism was selected from fermented foods. It was named as NU-7, and cultured in mushroom (Lentinus edodes, Shiitake) media. Optimal media to produce tyrosinase inhibitor was formulated by varing nitrogen or carbon content. If glucose content was in a range of 3-20% and ammonium sulfate was in a range of 0-0.25%, production of inhibitor was independent of cell mass. Addition of ammonium sulfate as a nitrogen source had little effect on inhibitor production. Production of inhibitor (Y) was proportionally related to shiitake content (X) with a regression equation of Y= -0.96X$^{2}$ + 13.07X + 14.43 (R = 0.96). These results indicate that shiitake and glucose are necessary for the production of tyrosinase inhibitor. In the analysis of mycotoxin in culture broth, aflatoxin was not detected, suggesting that it would be probably edible.

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