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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/17875

Title: 龜山島嗜高溫菌 Thermoanaerobacterium sp. NTOU2 醣類水解酵素第28家族之表現與特性鑑定
Expression and characterization of Glycosyl Hydrolase Family 28 from Thermoanaerobacterium sp. NTOU2
Authors: 廖吉隆
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Keywords: 果膠分解酶
polygalacturonase
Date: 2010
Issue Date: 2011-07-04
Abstract: 果膠分解酶屬於第28類型糖類分解酵素,Thermoanaerbacterium sp. NTOU2之果膠分解酶分析為polygalacturonase,主要分解直鏈半乳糖醛酸α-(1,4) –糖苷鍵(1,4-linked-α-galactosyluronic acid),直鏈半乳糖醛酸存在於果膠之平滑區域中,其分解能夠有效瓦解果膠結構。 果膠分解酶(pectinase)廣泛應用在多個工業處理過程上,處理果汁使之產量增加、澄清化、植物纖維的脫膠、以及處理含大量果膠之廢液。部分工業的製備過程都在中高溫度下進行,所以應用的酵素需要對中高溫具有較高耐受性,提升生產效率。 本研究果膠酶來源取自龜山島海底熱泉中的嗜高溫菌Thermoanaerbacterium sp. NTOU2,在基因體定序分析中具有果膠分解酶的基因序列,藉由其嗜高溫菌之特性,生產出具高溫穩定和耐受性的果膠酶。 經由基因序列、蛋白質胺基酸序列對比,表現出具有分解果膠能力並且有中高溫穩定性果膠酶,並做生化特性測試;Thermoanaerbacterium sp. NTOU2之果膠分解酶初步測試最適pH值為pH 5.5,最適溫度為60℃;Na、Mg、Ca離子會增加其活性,而K、Hg離子則產生抑制作用。
Pectinases hydrolyze α-1,4-linked-galactosyluronic acid, that existed in the smooth region of pectin, and destroy pectin structure. The enzyme are widely used in many industry, such as to improve the yield of juice extracts, clarify juice, the ret fiber crops, treat wastewater, etc. . Pectinases used in the industry must have the characteristics of tolerance of extreme conditions for increased the efficiency. Thermoanaerbacterium sp. NTOU2 is a thermophilic anaerobic bacterium, isolated from a acidic hydrothermal vent in the Gueishan Island near Taiwan. A polygalacturonase gene, named pgaseY, was identified from the genomic sequence of strain NTOU2. PGaseY belongs to glycosyl hydrolase family 28. For protein production, PGaseY was expressed in Pichia pastoris and the pectinase activity was detected in the culture medium. We collected culture medium for analysis of PGaseY’s biochemical properties. PgaseY showed the optimal pH at pH 5.5 and optimal temperature at 60℃. Na+, Mg2+, and Ca2+ was able to enhance the activity, whereas K+ and Hg2+ was able to decrease the activity of PGaseY. Because PGaseY shows remarkable characteristics, the enzyme may be analyzed more detail in the future.
URI: http://ethesys.lib.ntou.edu.tw/cdrfb3/record/#G0M97360029
http://ntour.ntou.edu.tw/ir/handle/987654321/17875
Appears in Collections:[生命科學暨生物科技學系] 博碩士論文

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