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Imprinted Cross-Linked Enzyme Aggregate (iCLEA) of Phenylalanine Ammonia Lyase: A New Stable Biocatalyst

机译:印迹交联酶聚集体(ICLEA)的苯丙氨酸氨裂解酶:一种新的稳定生物催化剂

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The industrial use of phenylalanine ammonia lyase (PAL), an interesting biocatalyst for manufacture of L-phenylalanine (L-Phe) by reversing the enzyme reaction with high concentration of trans-cinnamic acids (t-CA) and ammonia, has been hampered by a lack of long-term stability and low activity toward substrates. In this study, it is shown that the PAL activity of such a CLEA can be improved by molecular imprinting with a suitable substrate. PAL was imprinted with t-CA and subsequently cross-linked with glutaraldehyde (iCLEAs). Compared to free PAL, PAL stability in the iCLEAs against substrate inhibition was significantly improved, furthermore, the iCLEAs exhibited good reusability. These results indicated that the procedure might be used as a feasible and efficient solution for improving properties of immobilized enzyme in industrial application.
机译:苯丙氨酸氨裂解酶(PAL)的工业用途是通过逆转酶反应与高浓度的反肉桂酸(T-CA)和氨的酶反应制备L-苯丙氨酸(L-PHE)的有趣生物催化剂。缺乏长期稳定性和对基材的低活性。在该研究中,显示这种CLEA的PAL活性可以通过与合适的基材进行分子印刷来改善这种CLEA。 PAL印在T-CA并随后与戊二醛交联(ICLEAS)。与免费PAL相比,ICLEAS对基底抑制的PAL稳定性显着改善,ICLEAS表现出良好的可重用性。这些结果表明该方法可作为改善工业应用中固定化酶的性能的可行和有效的解决方案。

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