지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2013.1
- 수록면
- 427 - 433 (7page)
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초록· 키워드
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Glucoamylase (EC 3.2.1.3) is an important group of enzymes in starch processing, also referred to as amyloglucosidases, which are exo-acting amylases that release glucose from the non-reducing end of starch and related oligosaccharides. The glucoamylase newly isolated from the Aspergillus niger FME) was reported for the first time. This enzyme was produced by detergent-mediated release and purified to ~9.11 fold using Sephadex-G 100 and ion-exchange chromatography. Molecular mass of the glucoamylase was ~36 kDa as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The product of starch hydrolysis, analysed by thin-layer chromatography, showed the presence of glucose. The optimum pH and temperature for glucoamylase activity was 5.0 and $45^{\circ}C$, respectively. The $K_m$ and $V_{max}$ values of the enzyme were also determined using soluble starch as substrate as $94{\mu}g/mL$ and 39.02 U/mg, respectively. Moreover, glucoamylase was slightly activated by presence of Na and K ions and 10-20% inhibition was observed in presence of $Zn^{2+}$, $Sn^{2+}$, $Mg^{2+}$, $Ni^{2+}$, $Mn^{2+}$, and almost 80% with $Cu^{2+}$ ions, whereas the presence of ethylene diamine tetra acetic acid (EDTA) did not show significant inhibition. Glucoamylase, also assayed for surfactant property, shows significant surfactant tolerance at high concentrations of detergent and can retain 90% of its activity. Finally, secondary structure analysis of glucoamylase by circular dichroism spectroscopy showed the presence of 48% ${\alpha}$-helix, 11% ${\beta}$-sheet, and 41% random structure.
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