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- 저자 : 문금옥 ( Keum Ok Moon ) (검색결과 2 건)
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Cystein 처리 후 산화제 반응시간이 컬형성과 컬유지력에 미치는 영향
문금옥 ( Keum Ok Moon ),김순경 ( Soon Kyoung Kim ),김기영 ( Ki Young Kim ) 한국미용학회 2012 한국미용학회지 Vol.18 No.4
The aim of this study was evaluated the formation and sustainability of curl and hair damage minimization during the permanent waving. So that, sodium bromate and hydrogen peroxide as oxidant have been treated with cysteine on normal hair for 5-, 10-, 15- and 20- minutes and then the wave form, physicochemical properties and morphological change have been observed. As the results, optimal reaction time of oxidants has been confirmed as 20-minutes application of sodium bromate and 10-minutes application of hydrogen peroxide. When comparing two oxidants, hydrogen peroxide was excellent in formation rate of wave and sodium bromate was superb in curl sustainability. Considering the decrease in hair thickness was lower in sodium bromate than in hydrogen peroxide but was same in both 10-minutes treatment of sodium bromate and 20-minutes treatment of hydrogen peroxide. In addition, tensile strength was higher in treatment of hydrogen peroxide. When it comes to morphological observation of hair cuticle, hair damage turned out to be low because hydrogen peroxide with strong oxidizing capacity reacts to hair for a very short period of time. Therefore, it is considered that sodium bromate should be used to preserve elastic S-curl for a long time and to reduce the perm frequency and hydrogen peroxide should be treated to curtail the time required in permanent waving and to minimize hair damage.
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Microbacterium sp. AL-210이 생산하는 levan fructotransferase의 효소활성에 중요한 아미노산의 동정
성희경,문금옥,최기원,최경화,황경주,김묘정,차재호,Sung, Hee-Kyung,Moon, Keum-Ok,Choi, Ki-Won,Choi, Kyung-Hwa,Hwang, Kyung-Ju,Kim, Myo-Jung,Cha, Jae-Ho Korean Society of Life Science 2007 생명과학회지 Vol.17 No.1
[ $\beta$ ]-Fructofuranosidases, a family 32 of glycoside hydrolases (GH32), share three conserved domains including the W(L/M)(C/N)DP(Q/N), FRDPK, and ECP(D/G) motifs. The functional role of the conserved acidic residues within three domains of levan fructotransferase, one of the $\beta-fructofuranosidases$, from Microbacterium sp. AL-210 was studied by site-directed mutagenesis. Each mutant was overexpressed in E. coli BL21(DE3) and purified by using Hi-Trap chelating affinity chromatography and fast performance liquid chromatography. Substitution of Asp-63 by Ala, Asp-195 by Asn, and Glu-245 by Ala and Asp decreased the enzyme activity by approximately 100-fold compared to the wild-type enzyme. This result indicates that three acidic residues Asp-63, Asp-195, and Glu-245 play a major role in catalysis. Since the three acidic residues are present in a conserved position in inulinase, levanase, levanfructotransferase, and invertase, they are likely to have a common functional role as nucleophile, transition state stabilizer, and general acid in $\beta-fructofuranosidases$. 당 분해효소의 family 32 (GH32)에 속하는 $\beta-fructofuranosidase$는 3차구조를 근거로 볼 때 W(L/M)(C/N)DP(Q/N), FRDPK, 그리고 ECP(D/G) 부위를 포함하는 세 군데의 보전적인 영역을 가지고 있다. 이러한 $\beta-fructofuranosidase$ family에 속하는 Microbacterium sp. AL-210 유래 levan fructotransferase (LFTase)의 보전적인 산성 아미노산들의 역할이 특정위치 돌연변이법으로 검사되었다. 각각의 돌연변이체는 대장균인 E. coli BL21 (DE3)균주에서 발현되어 대량 생산되었고, 금속 친화 크로마토그래피법과 FPLC법으로 순수 정제되었다. wild-type LFTase의 효소의 활성은 0.74 unit 인 반면 네 개의 돌연변이체인 D63A, D195N, E245A, E245D 각각은 specific activity를 측정해 본 결과 원 균주와 비교해서 약 100배 정도 감소한 효소활성을 보여 주었다. 이로써 아미노산 변형의 target이 되었던 Asp-63, Aps-195, 그리고 Glu-245가 모두 효소 활성 및 기질과의 결합에 상당히 중요한 역할을 하고 있음이 판명되었다. 이러한 세 부위의 산성 아미노산들은 inulinase, levan fructotransferase와 invertase에 모두 보전적으로 위치 하므로 이들은 $\beta-fructofuranosidase$ family내 에서 공통된 역할을 할 것으로 사료된다.
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