Azlactone-reactive polymer supports for immobilizing synthetically useful enzymes. II. Important preliminary hydrogen bonding effects in the covalent coupling of Penicillin G Acylase
Azlactone-reactive polymer supports for immobilizing synthetically useful enzymes. II. Important preliminary hydrogen bonding effects in the covalent coupling of Penicillin G Acylase
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DOI：
10.1016/j.reactfunctpolym.2005.04.004
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发表时间：
2005-01-01
影响因子：
5.1
通讯作者：
Heilmann, SM
中科院分区：
文献类型：
--
作者：
Drtina, GJ;Haddad, LC;Heilmann, SM
研究了以氮杂内酯功能性分散体和反相悬浮聚合物载体作为青霉素酰化酶（PGA）的固定化介质。结果表明，最有效的载体是那些还含有伯和/或仲酰胺官能团。疏水相互作用和酰胺基团的支持和酶之间的氢键的组合，提出了提供重要的和密切的PGA和支持之间的共价偶联之前的关联。相对于环氧乙烷功能的商业标准，azlactonc生物催化剂载体具有更短的偶联时间和更高的催化活性。(C)2005 Elsevier B. V.保留所有权利。
Azlactone-functional dispersion and reverse phase suspension polymer supports were examined as immobilizing media for Penicillin G Acylase (PGA). Results indicated that the most effective supports were those that also contained primary and/or secondary amide functional groups. A combination of hydrophobic interactions and hydrogen bonding between amide groups on the support and enzyme was proposed to provide important and intimate association between PGA and support prior to covalent coupling. Relative to an oxirane-functional commercial standard, the azlactonc biocatalyst supports featured shorter coupling times and higher catalytic activities. (C) 2005 Elsevier B.V. All rights reserved.