以 SWISS-MODEL 的 伺 服 器 (http://swissmodel.expasy.org/) 建 立 rAFGAL 的三級結構，以推估的胺基酸序列搜尋相似的模板，得到最接近的模 板為 4fnq.1.A，為來自於 G. stearothermophilus 的 α-galactosidase AgaB，序列 相似度與覆蓋率分別為 55.69% 與 97%，為四聚體的結構，以此三級結構模 板建立 rAFGAL 的三級結構如圖四十四。
由 搜 尋 的 結 果 可 以 得 知 ， rAFGAL 與 G. stearothermophilus 的 α-galactosidase AgaB 親源性相當接近，過去的文獻指出 AgaB 為屬於 glycoside hydrolase family 36，且 Goh 學者將 A. kamchatkensis G10 的 α-galactosidase 歸類為 glycoside hydrolase family 36，由上述結果判斷 rAFGAL 應該屬於 glycoside hydrolase family 36 (Foucault et. Al., 2006; Goh et. Al., 2014)。
圖四十三、介面活性劑對 rAFGAL 酵素活性的影響。
Figure 43. Effects of detergents on the α-galactosidase activity of rAFGAL.
The activity assay was performed at 55oC in phosphate buffer with various 1 mM detergents for 30 min.
圖四十四、以 Swiss-model 所預測 rAFGAL 的三級結構。
Figure 44. Three-dimensional structure model of rAFGAL predicted by Swiss-model.
四、結論
arylamidase、α-chymotrypsin、α-galactosidase、α-glucosidase 與 β-glucosidase 的 活性皆為本研究中受測菌株最高者，且生長溫度最高可達 75oC，因此被選為酵 素選殖的對象。本研究成功從 A. flavithermus HY-TTH-D23 選殖出 subtilisin-type proteinase (rAFST) 與 α-galactosidase (rAFGAL) 的基因並轉入 E. coli BL21 (DE3) 中進行表現。其中 rAFST 可能由於自我催化降解而無法觀察到蛋白的表 Bacillaceae 科熱穩定 α-galactosidase 相較，純化產率為所有蛋白裡最高，並具 有最廣泛的 pH 活性範圍和最高的最適 pH。而比活性與最適溫度僅次於 G.stearothermophilus rAgaN。rAFGAL 為目前文獻中第一個從 Anoxybacillus spp.
中 選 殖 並 異 源 表 現 生 產 的 α-galactosidase 。 本 研 究 結 果 除 了 希 望 能 對 Anoxybacillus spp. 的 α-galactosidase 基本特性有所描述與貢獻外，未來還能應 用在食品、製糖與飼料等高溫工業製程。
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