KCI등재
大豆 및 Aspergillus niger α-galactosidase의 酵素學的 硏究 = Enzymatic Studies on the α-Galactosidases from Soybean and Aspergillus niger
저자
발행기관
학술지명
권호사항
발행연도
1991
작성언어
Korean
KDC
520
등재정보
KCI등재
자료형태
학술저널
수록면
49-73(25쪽)
제공처
소장기관
To elucidate enzymatic properties of α-galactosidases (EC3, 2. 1. 22) from germinated soybean and Aspergillus niger changes in the enzyme activities and oligosaccharide contents during germination of soybean were determined and α-galactosidases from germinated soybean and wheat bran culture of Aspergillus niger were purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. Their chemical and enzymatic properties were investigated and the results obtained were summarized as follows :
1. α-Galactosidase activity of soybean was maximized when it was germinated at 25℃ for 120 hours. And raffinose and stachyose in soybean were decomposed completely after 96 hours and 120 hours of germination. respectively.
2. The highest level of α-Galactosidase activity was obtained when Aspergillus niger was grown on wheat bran medium at 30℃ for 96 hours.
3. Soybean α-galactosidase was purified by6.6 fold by ammonium slufate 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.
4. Aspergillus niger α-galactosidase was purified by 23.7 fold. Its specific activity was 1,929 units/㎎ protein and the yield was 14% of the total activity of wheat bran culture.
5. The purified α-galactosidases of soybean and. Aspergillus niger were found to be homogeneous by polyacrylamide gel electrophoresis and by HPLC.
6. Chemical properties of the purified α-galactosidases were :
1) The soybean α-galactosidase was monomeric and its molecular weight was estimated to be 30.000 by SDS-PAGE whereas the Aspergillus niger α-galactosidase was a tetrameric glycoprotein which consisted of identical subunits with molecular weight of 28,000 each.
2) Isoelectric points of α-galactosidases were determined analytical isoelectric focusing to be : pH 4.8 for the soybean enzyme; and pH 4.6 for the Aspergillus niger enzyme, respectively.
3) Among the amino acids in active sites of both soybean and Aspergillus niger α-galactosidases, histidine was identified by chemical modification of diethyl pyrocarbonate. 1
4) The activity of soybean α-galatosidase was inhibited by 2-mercaptoethanol and L-cysteine.
7. Enzymatic properties of the purified α-galatosidases were :
1) The optimal temperature and pH for the α-galactosidase activity were : 40℃ and pH 6.0 for the soybean enzyme : and 40℃ and pH 6.5 for the Aspergillus niger enzyme.
2) The soybean α-galactosidase was stable at the range of pH 5.5 to 6.5 and at temperature below 45℃, however 75% of its activity was lost by heating at 60℃ for 10 min. The Aspergillus niger α-galactosidase was stable at the range of pH 6.0 to 7.0 and at temperature below 45℃, but 55% of its activity was lost under the same condition.
3) No significant difference was found in substrate specificity between (he bean and enzymes and both appeared to have higher affinity to raffinose than to stachyose. The enzymes were inhibited by galactose.
4) The Km values of soybean and Aspergillus niger enzymes were 5.3mM and 5.0mM for p-nitrophenyl-α-D-galactopyranoside, 50.0mM and 37.0mM for raffinose. and 55.5mM and 55.5mM for stachyose, respectively.
5) The activation energy and Q_10 value on p-nitrophenyl-α-D-galactopyranoside were calculated to be : 13.024 ㎉ per mole and 2.0 for the soybean enzyme; and 8.515 Kcal per mole and 1.38 for the Aspergillus niger enzyme.
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