酵素法生產N-乙醯甘露醣胺之研究

謝孟鋼

doi:10.6845/NCHU.2009.00438

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酵素法生產N-乙醯甘露醣胺之研究

Enzymatic process for the synthesis of N-Acetyl-D-Mannosamine

謝孟鋼 , Masters　　Advisor：林松池　　

繁體中文 DOI： 10.6845/NCHU.2009.00438

唾液酸；差向異構酶葡萄醣胺；異構化；固定化； Sialic acid ； N-acetyl-D-mannosamine ； N-actyl-D-glucosamine 2-epimerase ； epimerization ； immobilization.

Abstract │ Reference (56) │ Altmetrics

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Sialic acid, which plays a significant role in numerous biological functions, is an important precursor for the synthesis of many pharmaceutical drugs such as anti-influenza virus agents. Enzymatic process employing N-acetyl-D-neuraminic acid (NeuAc) aldolase for the synthesis of sialic acid from N-acetyl-D-mannosamine (ManNAc) and pyruvate has been reported. To reduce substrate costs, an alternative process with N-acetyl-D-glucosamine (GlcNAc) and GlcNAc 2-epimerase as the catalysts has been proposed, enabling the use of relatively inexpensive GlcNAc instead of ManNAc as the starting reactant. In this study, we report the enzymatic production of ManAc from GlcNAc with immobilized recombinant porcine kidney GlcNAc 2-epmerase. GlcNAc 2-epimerse, a homo-dimeric protein with a molecular weight of 84 kDa, was immobilized onto Eupergit C, a commercial oxirane-based support with reactive amino groups. A maximal enzyme load of 1.0 mg/g gel was achieved. The effect of enzyme load on the specific activity of the immobilized 2-epimerase was investigated. At an optimal enzyme load of 0.41 mg/g gel, a specific activity of 2.87 IU/mg epimerase, approximately 33 % lower than that of the free enzyme, was obtained. Further increase in enzyme load led to a decline in enzyme specific activity. Surprisingly, the optimal reaction temperature of the enzyme, 60 oC, was not increased upon immobilization. Nevertheless, the immobilized activity did exhibit a higher activity at elevated temperature. A higher residual activity of 47.8 % was observed for the immobilized epimerase at 80 oC than that for the free enzyme, 14.7 %.  The thermal stability of the enzyme was also significantly enhanced upon immobilization. While incubating at 80 oC for 5 h completely inactivated the free enzyme, a residual activity of 20.9 % was obtained for the immobilized enzyme. The pH profile of the immobilized enzyme is similar to that of the free enzyme. The reusability of the immobilized enzyme in a batch reactor was also studied. A residual activity of 63.8 % was obtained after 24 cycles. The effect of space time on conversion in a continuous packed-bed reactor will also be discussed

Reference ( 56 ) 〈TOP〉

吳冠毅 (2006) 。雙硫鍵對差向異構酶熱穩定性之影響。碩士論文，化學工程研究所，中興大學，台中。
連結：
顏敏智(2007) 。以固定化酵素生產L-同苯丙胺酸。碩士論文，化學工程研究所，中興大學，台中。
連結：
李晏忠 (2007) 。N-acetyl-D-glucosamine 2-epimerase 之生化及結構分析俾應用於酵素法生產N-acetyl-D-neuraminic acid。博士論文，分
連結：
Maru, I., J. Ohnishi, Y. Ohta, and Y. Tsukada, “Simple and large-scale production of N-acetylneuraminic acid from N-acetyl-D-glucosamine and pyruvate using N-acyl-D-glucosarnine 2-epimerase and N- acetylneuraminate lyase,”J. Biosci. Bioen ., 306, 575-578 (1998) .
連結：
sialidase-based inhibitors of influenza virus replication.” Nature., 363
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