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- 저자 : 金鍾和(Kim Jong Hwa) (검색결과 11 건)
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대두 ${\alpha}-galactosidase$의 정제 및 성질
금종화,오만진,김성렬,Keum, Jong-Hwa,Oh, Man-Jin,Kim, Seong-Yeol 한국응용생명화학회 1991 Applied Biological Chemistry (Appl Biol Chem) Vol.34 No.3
To elucidate enzymatic properties of ${\alpha}-galactosidase$ (EC 3, 2, 1, 22) from germinated soybean, changes in the enzyme activities and oligosaccharide contents during germination of soybean were determined. ${\alpha}-Galactosidase$ from germinated soybean was purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. Their chemical and enzymatic properties was investigated. ${\alpha}-galactosidase$ activity of sobeam was maximized when it was germinated at $25^{\circ}C$ for 120 hour. Raffinose and stachyose in soybean were decomposed completely after 96 hours and 120 hours of germination, respectively. Soybean ${\alpha}-galactosidase$ was purified by 6.6 fold by ammonium sulfate fractionation, ion exchange chromatography on DEAE-Cellulose and Sephadex A-50, and gel filtration on Sephadex G-150. Its specific activity was 825 Units/mg protein and the yield was 2.5% of the total activity of crude extracts. The purified ${\alpha}-galactosidase$ of soybean was found to be homogeneous by polyacrylamide gel electrophoresis and by HPLC. Isoelectric point of soybean ${\alpha}-galactosidase$ was determined analytical isoelectric focusing to be pH 4.8. The soybean ${\alpha}-galactosidase$ was monomeric and its molecular weight was estimated to be 30,000 by SDS-PAGE. The optimal temperature and pH for the soybeam ${\alpha}-galactosidase$ activity were $40^{\circ}C$ and pH 6.0 and 75% of its activity was lost by heating at $60^{\circ}C$ for 10 min. The enzyme was appeared to have higher affinity to raffinose than to stachyose. The Km value of soybean enzyme was 5.3 mM for ${\rho}-nitrophenyl-{\alpha}-D-galactopyranoside$ and the activation energy on PNPG was calculated to be 13.02 Kcal per mole. 대두 발아 과정 중의 ${\alpha}-galactosidase$를 추출하여 염석, 이온교환 크로마토그래피 및 겔 여과 등의 방법으로 정제한 후 정제효소의 효소학적 성질을 검토하였다. 대두 ${\alpha}-galactosidase$의 활성은 $25^{\circ}C$에서 120시간 발아시켰을 때 가장 높았으며, 대두 중의 raffinose는 96시간, stachyose는 120시간 발아시켰을 때 완전히 분해되었다. 대두 ${\alpha}-galactosidase$는 황산암모늄염석, DEAE-Cellulose 및 DEAE-Sephadex A-50 이온교환 크로마토그래피, Sephadex G-150 겔 여과 등에 의하여 비활성은 825U/mg protein으로써 6.6배까지 정제되었으며 수율은 2.5%이었고 HPLC와 PAGE에 의하여 순도를 확인하였다. 정제효소의 등전점은 pH 4.8이었고, 분자량은 30,000인 monomer이었으며 정제효소의 최적작용 PH는 6.0, 최적작용온도는 $40^{\circ}C$ 이었고, $60^{\circ}C$에서 10분 처리시 25%의 잔존 활성을 나타내었다. 정제효소는 stachyose보다 raffinose를 쉽게 분해하였으며 PNPG에 대한 Km값은 5.3 mM, 활성화 에너지는 13.02 cal/mole이었다.
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몇종의 세균과 Saccharomyces cerevisiae에 대한 식품첨가물의 향균 특성
이종수,오준세,김나미,금종화,이석건,Lee, Jong-Soo,Oh, Jun-Sei,Kim, Na-Mi,Keum, Jong-Hwa,Lee, Suk-Kun 배재대학교 자연과학연구소 1996 自然科學論文集 Vol.8 No.2
현재 식품첨가물로 많이 사용되고 있는 유기산과 안정제 및 색소 등의 각종 세균과 Sacch. cerevisiae 에 대한 향균 특성을 조사하였다. 산도 조절용으로 사용되고 있는 젖산, 사과산, 호박산 및 주석산은 L. acidophilus와 Sacch. cerevisiae에 대하여 향균성이 없었으나 B. subtilis등의 세균에 대하여는 향균성이 있었고 특히 사과산은 P. aeruginosa에 대하여 강한 향균력이 있었다.(최소생육저지농도 : 0.05%). 안정제로서의 알긴산과 펙틴은 B. subtilis, E. coli, P. aeruginosa에 대하여 비교적 강한 향균성을 보였고 L. acidophilus에 대하여는 향균성이 없었다. 황색 색소(홍화엘로우)와 적색 색소(Red powder-N)는 향균성이 없었고 표백제인 $NaHSO_3$의 세균에 대한 최소생육저지농도는 0.05%, Sacch. cerevisiae에 대하여는 0.5%로 향균성이 있었다. In order to survey the safety of some food additives, antimicrobial activity of acidulants, stabilizers, antioxidants, natural coloring materials and bleaching agents against 5 strains of bacteria and Sacch. cerevisiae were investigated by dilution method and minimal inhibitory concentration(MIC) method. Malic acid as acidulants displayed the effective antimicrobial activity in vitro against P. aeruginosa and its MIC is 0.05%. Alginic acid and pectin as stabilizer also displayed strong antimicrobial activity against B. subtilis, E. coli and P. aeruginosa, and tannin(antioxidants) and $NaHSO_3$ displayed antimicrobial activity against all bacteria tested. However gums(Arabia, Xanthan, Gua) and natural coloring materials(Hongwha Yellow, Red powder-N) were not affected to growth of bacteria and Sacch. cerevisiae.
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Aspergillus niger α-Galactosidase의 정제 및 성질
금종화,오만진,김찬조 한국산업미생물학회 1991 한국미생물·생명공학회지 Vol.19 No.5
Aspergillus niger가 생산하는 α-glactosidase의 효소학적 성질을 조사하기 위하여 시험균주를 밀기울 배양한 후 생성된 α-glactosidase를 염석, 이온교환 크로마토그래피 및 겔 여과 등의 방법으로 정제한 후 정제효소의 효소학적 성질을 검토하였다. Asp. niger를 밀기울 배지에서 30℃, 4일 배양했을 때 효소활성이 가장 높았으며 α-glactosidase는 황산암모늄 염석, DEAE-cellulose 및 DEAE-Sephadex A-50 이온교환 크로마토그래피, Sephadex G-150 겔 여과 등에 의하여 23.7배까지 정제되었으며 비활성이 1,220 U/㎎·protein, 수율 14%이었고 HPLC와 PAGE에 의해 순도가 확인되었다. 정제효소는 당 단백질로서 등전점은 4.6이었고 분자량이 28,000인 monomer 4개로 구성된 tetramer이었다. 정제효소의 최적작용 pH는 6.5, 최적작용온도는 40℃이었고 60℃에서 10분 처리시 46%의 잔존활성을 나타내었다. 정제효소는 stachyose보다 raffinose를 쉽게 분해하였고 PMPG에 대한 K_m값은 5.0mM, 활성화에너지는 8.515Cal/mole이었다. To elucidate enzymatic properties of α-glactosidase(EC 3.2.1.22) from Asp. niger, α-glactosidase from wheat bran culture was purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. And then its enzymatic propeties were investigated. The highest level of α-glactosidase activity was obtained when Asp. niger was grown on wheat bran medium at 30℃ for 96 hours. The α-glactosidase was purified by 23.7 fold by ammonium sulfate fractionation, ion exchange chromatography on DEAE-Celluose and Sephadex A-50, and gel filtration on Sephadex G-150 and its specific activity was 1,229 Units/㎎ protein and the yield was 14% of the total activity of wheat bran culture. The purified α-glactosidase was found to be homogeneous by polyacrylamide gel electrophoresis and HPLC. The α-glactosidase was a tetrameric glycoprotein which consisted of identical subunits with molecular weight of 28,000 each by SDS-PAGE and isoelectric point was determined analytical isoelectric focusing to be pH 4.6. The optimal temperature and pH for the α-glactosidase activity were 40℃ and pH 6.5, respectively, and 54% of its activity was lost by heating at 60℃ for 10 mins. It was appeared to have higher affinty to raffinose than to stachyose. The K_m value and activation energy of α-glactosidase were 5.0 mM and 8.515㎉ per mole for p-nitrophenyl-α-D-galactopyranoside, respectively.
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대두 α - galactosidase 의 정제 및 성질
오만진,금종화,김성렬 한국농화학회 1991 Applied Biological Chemistry (Appl Biol Chem) Vol.34 No.3
To elucidate enzymatic properties of α-galactosidase (EC 3, 2, 1, 22) from germinated soybean, changes in the enzyme activities and oligosaccharide contents during germination of soybean were determined. α-Galactosidase from germinated soybean was purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. Their chemical and enzymatic properties was investigated. α-galactosidase activity of sobeam was maximized when it was germinated at 25℃ for 120 hour. Raffinose and stachyose in soybean were decomposed completely after 96 hours and 120 hours of germination, respectively. Soybean α-galactosidase was purified by 6.6 fold by ammonium sulfate fractionation, ion exchange chromatography on DEAE-Cellulose and Sephadex A-50, and gel filtration on Sephadex G-150. Its specific activity was 825 Units/㎎ protein and the yield was 2.5% of the total activity of crude extracts. The purified α-galactosidase of soybean was found to be homogeneous by polyacrylamide gel electrophoresis and by HPLC. Isoelectric point of soybean α-galactosidase was determined analytical isoelectric focusing to be pH 4.8. The soybean α-galactosidase was monomeric and its molecular weight was estimated to be 30,000 by SDS-PAGE. The optimal temperature and pH for the soybeam α-galactosidase activity were 40℃ and pH 6.0 and 75% of its activity was lost by heating at 60℃ for 10 min. The enzyme was appeared to have higher affinity to raffinose than to stachyose. The Km value of soybean enzyme was 5.3 mM for ρ-nitrophenyl-α-D-galactopyranoside and the activation energy on PNPG was calculated to be 13.02 K㎈ per mole.
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