• Food Science and Preservation
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• v.25 no.1
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• pp.79-89
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• 2018

In this study, the anti-oxidant, whitening, and anti-wrinkle effects of Castanea crenata inner shell extracts processed by enzyme treatment and pressurized extraction were investigated. The Castanea crenata inner shell was first hydrolyzed using celluclast, viscozyme, or hemicellulase. Then, it was subjected to pressure extraction for different durations (30, 60, and 120 min). The yields of the Castanea crenata inner shell extracts processed by different enzyme treatments followed by pressurized extraction for different times are in the range of 12.42-29.80%. The total polyphenol, flavonoid, and tannin contents of the C30m (celluclast enzyme and autoclave extracts at 30 min) extract were 15.48, 10.82, and 15.82 g/100 g, respectively. The total sugar content of the H120m(hemicellulase enzyme and autoclave extracts at 120 min) extract is 61.07 g/100 g. The 1,1-diphenyl-2-pycrylhydrazyl (DPPH) and 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activities of the C30m extract at $1,000{\mu}g/mL$ are 89.20, and 81.96%, respectively. The superoxide radical scavenging and ferric-reducing antioxidant power of the C30m extract at $1,000{\mu}g/mL$ are 67.63% and $1,324.79{\mu}M$, respectively. Further, the tyrosinase and elastase inhibition activity of the C30m extract at $1,000{\mu}g/mL$ are 61.32, and 61.06%, respectively. Our results indicate that the Castanea crenata inner shell extracts processed by enzyme treatment followed by pressurized extraction could have beneficial effects on facial skin and they should be considered for use in new functional cosmetics.

• 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.

• 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.