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題 名 | 幾丁聚醣酶之研究現況=The Recent Study of Chitosanase |
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作 者 | 傅安庭; | 書刊名 | 親民學報 |
卷 期 | 12 民95.07 |
頁 次 | 頁11-20 |
分類號 | 346.217 |
關鍵詞 | 幾丁聚醣酶; 幾丁聚醣; β-1,4醣苷鍵; |
語 文 | 中文(Chinese) |
中文摘要 | 幾丁聚醣酶(chitosanase;EC 3.2.1.99)能水解完全或部份去乙醯之幾丁聚醣,其作用位置在幾丁聚醣β-1,4醣苷鍵,可將幾丁聚醣水解為幾丁寡醣及葡萄糖胺。目前已知在細菌、真菌、植物、無脊椎動物,甚至脊椎動物(包括人類)都發現有幾丁聚醣酶之存在。許多微生物中甲殼分解酶之基因與酵素已被篩選出來,但在基因序列比對上、分子量及蛋白質水解後之產物都不盡相同。然而幾丁聚醣酶在結構上具有相似的催化區域,可以參與一個或多個幾丁聚醣鍵結區域進而使受質內之氫鍵瓦解進而加速受質被酵素催化而分解。目前尚未發現良好之幾丁聚醣酶能將幾丁聚醣催化成為六聚醣體,因此試圖篩選具催化成六聚醣體本土性之微生物以供醫療使用。 |
英文摘要 | Chitosanases (EC 3.2.1.99) are hydrolases acting on chitosan which is linear polysaccharide of β-1,4-linked D-glusecosamine residue. They are found in bacteria, fungi, plants, invertebrates, and all classes of vertebratcs including human. These enzymes hydrolyze the abundant natural biopolymer chitin, producing smaller chito-oligosaccharides. Many chitinases have been isolated, and several genes encoding these enzymes have also been cloned from a wide variety of bacteria. Some of these bacteria have been reported to produce multiple forms of chitinases with different molecular masses, and such multiplicity is preseumed to be due to the presence of different genes, or proteolytic modifications of a single gene product. Many chitinases are composed of a catalytic domain joined to one or more chitin-binding domains. This kind of substrate-binding domain is functional not only for accumulating catalytic sites on the surface of substrates but also for disrupting hydrogen bonds in the crystalline region of substrates and thereby facilitating subsequent hydrolysis by the catalytic domains. The chitin-oligosaccharides are soluble in water and can be absorbed by intestine. Usually, the activity is the most apparent in human body with hexamers. There is no useful chitinase to product the hexmers until now, so it is important to screen the local bacteria with this kind activity of chitinase. |
本系統中英文摘要資訊取自各篇刊載內容。