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|標題:||疊氮化鈉誘變菜豆之α-amylase inhibitor 1純化與其活性之探討
Purification and activity of α-amylase inhibitor 1 from NaN3-induced common bean mutants
|關鍵字:||common bean;菜豆;α-amylase inhibitor;NaN3 mutation;protein purification;α-澱粉分解沒抑制物;疊氮化鈉誘變;蛋白質純化||出版社:||農藝學系所||引用:||胡懋麟。1994。菜豆。出自”雜糧作物各論”，蔡文福主編，pp. 1269-1281。台北：財團法人台灣區雜糧發展基金會。 葉茂生。2009。食用作物學。國立中興大學農藝學系。台中。 Abe, J. I., U. Sidenius, and B. Svensson. 1993. Arginine is essential for the α-amylase inhibitory activity of the α-amylase/subtilisin inhibitor (BASI) from barley seeds. Biochem. J. 293: 151-155. Acosta-Gallegos, J. A., J. D. Kelly,.and P. Gepts. 2007. Prebreeding in common bean and use of genetic diversity from wild Germplasm. Crop Sci. 47: S-44-S-59. Aubry, C., M. C. Morere-Le Paven, A. L. Chateigner-Boutin, B. Teulat-Merah, C. Ricoult, D. Peltier, R. Jalouzot, and A. M. Limami. 2003. A gene encoding a germin-like protein, identified by a cDNA-AFLP approach, is specifically expressed during germination of Phaseolus vulgaris. Planta 217: 466-475. Bloch Jr, C., and M. Richardson. 1991. 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菜豆（Phaseolus vulgaris L.）種子內含有澱粉分解酶抑制物 （α-amylase inhibitor 1, α-AI1），能與豬胰臟型澱粉分解酶、人胰臟型澱粉分解酶結合，從而抑制澱粉分解，因此α-AI1可用於改善二型糖尿病的惡化或肥胖症的發生。本研究利用三相分離法（three-phase partitioning, TPP），首先將菜豆粗萃取液pH值調整至5.25後，加入30%飽和硫酸銨以沈澱蛋白，再以1:1 (v/v) 加入第三級丁醇（t-butanol）產生三相，於水層得到純化之α-AI1，其中引種之白腎豆（PI-40）與台灣花豆花莢種（Hwachia），經TPP步驟後可得純化倍數（purification fold）分別為7.6與18倍，而α-AI1總活性仍能維持80與66%。本研究接著以擴增片段長度多型性（amplified fragment length polymorphism, AFLP）分析34個NaN3之菜豆誘變品系，求得各品系間之遺傳變異程度，從中挑選9個菜豆誘變品系與引種之菜豆以TPP系統進行α-AI1之純化，並檢測α-AI1之活性。結果發現菜豆誘變品系SA-05之α-AI1對α-amylase具有較高的抑制活性，可供未來商業化生產α-AI1之參考。
Common bean (Phaseolus vulgaris L.) contain α-amylase inhibitor 1 (α-AI1), which would bind α-amylase and subsequently reduce starch digestion. Thus, α-AI1 can be used to control the deterioration of type II diabetes and obesity. In this study, a three-phase partitioning (TPP) technique was used to extract and purify α-AI1 from common bean. The crud extracts were adjusted to pH 5.25, and 30% ammonium sulfate was added. Then the tert-butanol was added to the mixing solution for obtaining three phases. The results indicated that the α-AI1 proteins were mainly recovered in the aqueous phase. The purified α-AI1 for varieties PI-40 and Hwachia were 7.6 fold and 18 fold, respectively. The recovery of total activity was 81 % and 66 %, respectively, for PI-40 and Hwachia. AFLP (amplified fragment length polymorphism) was subsequently used to assess genetic diversity among Hwachia and it 34 NaN3-induced mutants. Nine NaN3-induced mutants and Hwachia and 2 introduced varieties used for α-AI1 purification by using TPP and then the α-AI1 inhibitor activity was determined. The results showed that the mutant SA-05 had higher inhibitor activity than other NaN3-induced mutants and Hwachia. Thus, mutant SA-05 may be useful in commercial preparation of α-AI1.
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