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In Situ Calb Enzyme Immobilization in Mesoporous Material Type MCM-48 Synthesis Using Ionic Solid [C14MI]Cl as Structure-Directing Agent
Applied Biochemistry and Biotechnology ( IF 3 ) Pub Date : 2021-09-15 , DOI: 10.1007/s12010-021-03648-z
Catia S Zanchett Battiston 1, 2 , Aline M Moreira Ficanha 2, 3 , Carolina E Demaman Oro 2 , Rogério Marcos Dallago 2 , Marcelo Luis Mignoni 2
Affiliation  

MCM-48 mesoporous support was synthesized with the ionic solid 1-tetradecyl-3-methylimidazolium chloride ([C14MI]Cl) as a structure-directing agent for in situ immobilization of Candida antarctica B (CALB). The MCM-48[C14MI]Cl support showed characteristics of mesoporous material of interest, with a pore size of 20.30 and 73.41 A for the support without and with the enzyme, respectively. The elongation of the carbonic chain of the ionic solid directly influenced the increase in the specific area and pore volume of the material. In addition, the decrease in the specific area and pore volume for support with the enzyme showed the effectiveness of immobilization in situ. It was possible to obtain the ideal levels for the best activities of esterification of the enzyme with optimization of a mathematical model. The optimized variables were 0.31 g of enzyme and 3.35% of ionic solid with a maximum esterification activity of 392.92 U/g and 688% of yield. The support showed residual activity above 50% when stored under refrigeration for 75 days. At 60 and 80 °C, the enzyme immobilized on the support retained more than 80 and 40% of its residual activity, respectively. In addition, the support presented the possibility of reuse for up to 10 cycles with residual activity of approximately 50%. The support synthesized in the present study presents a great industrial opportunity for the immobilization and use of the CALB enzyme.



中文翻译:

使用离子固体 [C14MI]Cl 作为结构导向剂的介孔材料类型 MCM-48 合成中的原位 Calb 酶固定化

以离子固体 1-十四烷基-3-甲基咪唑氯化物 ([C 14 MI]Cl) 作为结构导向剂,用于原位固定南极念珠菌B (CALB),合成了 MCM-48 介孔载体。MCM-48[C 14MI]Cl 载体显示出感兴趣的介孔材料的特征,对于不含酶和含酶的载体,孔径分别为 20.30 和 73.41 埃。离子固体碳链的伸长直接影响材料比面积和孔容的增加。此外,酶载体的比面积和孔体积的减少表明原位固定的有效性。通过优化数学模型可以获得酶的最佳酯化活性的理想水平。优化后的变量为 0.31 g 酶和 3.35% 的离子固体,最大酯化活性为 392.92 U/g,产率为 688%。当在冷藏下储存 75 天时,该载体显示出高于 50% 的残留活性。在 60 和 80 °C 时,固定在载体上的酶分别保留了超过 80% 和 40% 的剩余活性。此外,该支持提供了重复使用多达 10 个循环的可能性,剩余活性约为 50%。本研究中合成的载体为 CALB 酶的固定化和使用提供了巨大的工业机会。

更新日期:2021-09-15
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