Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions.

Immobilization of Mucor miehei Lipase onto Macroporous Aminated Polyethersulfone Membrane for Enzymatic Reactions.
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DOI:
10.3390/membranes2020198
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发表时间:
2012-04-12
期刊:
影响因子:
4.2
通讯作者:
Zulfikar MA
Zulfikar MA
中科院分区:
工程技术4区
文献类型:
--
作者:
Handayani N;Loos K;Wahyuningrum D;Buchari;Zulfikar MA

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酶的固定化是提高酶的稳定性、回收率和重复使用性的最有前途的方法之一。然而,研究合适的固定化酶的固体载体仍然是一个科学挑战。合成了聚醚砜(PES)和胺化聚醚砜(PES-NH 2)作为新型固定化材料。基于合成的PES和PES-NH 2聚合物,成功地制备了具有不同孔径(从10-600 nm)的膜,以应用于生物反应器来提高固定化脂肪酶的性能。研究了孔径、添加剂浓度以及PES骨架上连接的官能团对酶载量和酶活性的影响。通过固定在由10%的PES-NH 2、8%的邻苯二甲酸二丁酯(DBP)和5%的聚乙二醇(PEG)组成的PES-NH 2膜上的米黑毛霉脂肪酶获得最大的酶负载(872.62 μg/cm 2)。固定化脂肪酶的水解活性表明,固定化没有显著降低生物催化剂的活性。重复使用性试验表明,PES-NH 2固定化脂肪酶的稳定性好于PES固定化脂肪酶(PES-NH 2和PES固定化脂肪酶的活力回收率分别为97.16%和95.37%),表明这种新型材料具有作为酶反应生物反应器开发的潜力。
Immobilization of enzymes is one of the most promising methods in enzyme performance enhancement, including stability, recovery, and reusability. However, investigation of suitable solid support in enzyme immobilization is still a scientific challenge. Polyethersulfone (PES) and aminated PES (PES–NH2) were successfully synthesized as novel materials for immobilization. Membranes with various pore sizes (from 10–600 nm) based on synthesized PES and PES–NH2 polymers were successfully fabricated to be applied as bioreactors to increase the immobilized lipase performances. The influence of pore sizes, concentration of additives, and the functional groups that are attached on the PES backbone on enzyme loading and enzyme activity was studied. The largest enzyme loading was obtained by Mucor miehei lipase immobilized onto a PES–NH2 membrane composed of 10% of PES–NH2, 8% of dibutyl phthalate (DBP), and 5% of polyethylene glycol (PEG) (872.62 µg/cm2). Hydrolytic activity of the immobilized lipases indicated that the activities of biocatalysts are not significantly decreased by immobilization. From the reusability test, the lipase immobilized onto PES–NH2 showed a better constancy than the lipase immobilized onto PES (the percent recovery of the activity of the lipases immobilized onto PES–NH2 and PES are 97.16% and 95.37%, respectively), which indicates that this novel material has the potential to be developed as a bioreactor for enzymatic reactions.