• 대한화장품학회:학술대회논문집
• /
• 대한화장품학회 2003년도 IFSCC Conference Proceeding Book II
• /
• pp.50-59
• /
• 2003

BMB-CF has been constituted of purified fractions of Scutellaria baicalensis, which has medicinal effect such as anti-microbial. anti-inflammation. fever remedy. anti-oxidation. and anti-aging effect etc.. It has been used in traditional medicine formula from long time ago in the east Asia. It is constituted of the active flavone ingredients such as baicalin. baicalein. DTF(Di-methyl Tetra -hydroxy Flavone), wogonin. wogonoside. $\beta$- Sitosterol. etc.. General purified fractions of Scutellaria baicalensis has the high portion of the baicalin which has the problem of narrow antimicrobial spectrum and compatibility against cosmetic formula. Now. we has been develop the new purificaton process of Scutellaria baicalensis that has the high rate of DTF content, which is improved in antimicrobial activity and cosmetics compatibility. So. we have assure that it is the potent preservative against various cosmetic formula.

• KSBB Journal
• /
• 제9권2호
• /
• pp.115-121
• /
• 1994

240ml의 시료를 정제할 수 있는 30channel의 preparative-scale 자유유동전기이동 분리장치를 제작한 후 렌즈콩으로부터 lentil lectin(LcH)을 전기 집속법으로 분리하였다. 분리된 각 분획을 PAGIEF젤에서 silver staining했을 때 불순물이 전혀 검출되지 않을 정도의 고순도 lectin을 얻을 수 있었다. 이 때 ampholyte로서 HEPES(50mM) -Tris(50mM) -urea(3M) 등을 사용하였으며 50mM Histidine(pI 7.65)인 경우 가장 분리도가 가장 좋았다. LcH는 보통의 조건하에서 LcH-A와 LcH-B의 두가지 순수한 형태로만 나타났으며 따라서 이 장치를 사용하여 다단 분리 정제를 할경우 두 성분의 완전한 분리도 가능함을 보여 주었다.

• Journal of Microbiology and Biotechnology
• /
• 제1권3호
• /
• pp.188-196
• /
• 1991

The ${\beta}-glucosidase$ was purified to homogeneity from the culture filtrate of P. verruculosum by column chromatography. The enzyme was a glycoprotein with a relative size of approximately 220 kDa with an isoelectric point of 4.8, which was composed of dimeric protein of 105 kDa. The enzyme was stable up to $60^{\circ}C$ and the presence of glycerol significantly increased its thermostability. The enzyme was found to hydrolyze both ${\beta}-aryl$ and ${\beta}-alkyl-glucosides$ in addition to ${\beta}-glucosyl$ glucose and catalyzed glucosyl transfer to cellobiose. The enzyme attacked laminarin in an exotype-like fashion. The apparent Km's of the enzyme toward cellobiose, laminaribiose, laminarin were 0.53 mM, 0.35 mM and 1.11 mM, respectively. Glucose and glucono-${\delta}-lactone$ were competitive inhibitors for the enzyme. Copper ($Cu^{2+}$), mercury ($Hg^{2+}$) and p-chloromercuribenzoate were strong inhibitors of the enzyme. The immunoblotting result revealed that one form of ${\beta}-glucosidase$ was biosynthesized, irrespective of carbon sources used. Polyacrylamide gel electrophoresis analysis of the in vitro translated product of total RNA from avicel grown mycelium established that the P. verruculosum ${\beta}-glucosidase$ precursor was approximately 95 kDa in size. The amino acid composition and N-terminal amino acid sequence are given.

• 생약학회지
• /
• 제30권3호
• /
• pp.306-313
• /
• 1999

Polyphenol Oxidase(PPO) was purified from an extract of Ginkgo biloba leaves by ammonium sulfate fractionation followed by sephadex G-150 column chromatography, which resulted in a 18-fold increase in specific activity. The enzyme was most active at pH 8.5 and the temperature optimum for the PPO catechol oxidation reaction was $45^{\circ}C$. Heat inactivation studies showed that heating for 7, 9 and 48 min, at 80, 70 and $60^{\circ}C$ respectively caused a 50% loss in enzymatic activity and that the enzyme was completely inactivated after heat treatment at $90^{\circ}C$ for 60 min. Km values of the PPO for catechol, hydroquinone and 4-methylcatechol derived from Lineweaver-Burk plots were $6.06\;{\times}\;10^{-4}M,\;1.02\;{\times}\;10^{-3}M,\;1.41\;{\times}\;10^{-3}M$ respectively. Of the substrates tested, 4-methylcatechol was oxidized most readily and the enzyme did not oxidize monophenols. The enzyme datalyzed browning reaction was completely inhibited in the presence of reducing reagents, namely ascorbic acid, cysteine, glutathione, 2-mercaptoethanol, potassium metabisulfite at 0.5 mM level. Sodium chloride showed very little inhibition effect on Ginkgo biloba leaves PPO. Lineweaver-Burk analysis of inhibition data revealed that the inhibition by cysteine, 2-mercaptoethanol, potassium cyanide was competitive with ki values of $1.1\;{\times}\;10^{-5}M,\;2.4\;{\times}\;10^{-5}M,\;8\;{\times}\;10^{-5}M$, respectively. Among the divalent cations, $Cu^{2+}ion$ was a strong activator on PPO and $Mn^{2+}ion$ was little or no effect on PPO activity $Ni^{2+}ion$ was an inhibitor on PPO.

• 한국식품과학회지
• /
• 제26권5호
• /
• pp.633-637
• /
• 1994

퇴비에서 maltotetraose 생산성 아밀라제를 분비하는 세균 KSM-35를 분리하여 그의 형태적, 생화학적 특성을 고려하여 Steptomyces albus로 잠정 동정 하였다. 이 균주가 생산하는 아밀라제는 유안침전 분획, DEAE-Toyo pearl 및 2회의 sephadex-100 크로마토그라피로 44.5배 정제하며 27.1%의 활성을 회수할 수 있었다 이 효소의 등전점은 4.3이었으며 SDS-PAGE로 분석한 결과 분자량은 약 50,000이었다. 이 균주의 아밀라제를 2% 전분과 26시간 반응시킨 후 생성된 올리고당류를 HPLC로 조사한 결과 56%가 maltotetraose로서 주산물이었고 maltose와 maltoriose가 각각 20% 및 16%를 차지하였으며 기타 소량의 glucose, maltopentaose가 검출되었다.