| Title | Schwanniomyces castellii glucoamylase의 정제 및 성질 | ||
| Author | 배석 · 박종천 · 김동호 * · 김강화 ** · 전순배 | ||
| Address | 전남대학교 미생물학과; * 생물학과; ** 식품영양학과 | ||
| Bibliography | Korean Journal of Microbiology, 29(2),104-110, 1991 | ||
| DOI | |||
| Key Words | Schwanniomyces castellii, glucoamylase | ||
| Abstract | The glucoamylase of Schwanniomyces castellii was purified to homogeneity from the culture filtrate. the purified enzyme was a glycoprotein with a molecular mass of about 145 KDa, which was monomeric protein with an isoelectric point of 4.3. The pH and temperature optima were 5.5 and 40℃, respectively. The enzyme was fairly stable up to 50℃ and at acid pH range (pH 4.5-6.0). The apparent Km of the enzyme toward soluble starch, isomaltose and pullulan were 3.84, 0.51 and 13.7 mg/ml, respectively. The analysis of amino acid composition on this enzyme was found to be acidic protein like other fungal glucoamylase. The amino acid sequence of N-terminal peptide consisted of Ala-Pro-Ala-Asp-Gly-Ile-Gly-Asp-X-Ala-X-Ala. | ||
| Download PDF | Kor_290206_104-110p.pdf | ||