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Immobilization of Thermoalkalophilic Lipase from Bacillus atrophaeus FSHM2 on Amine-Modified Graphene Oxide Nanostructures: Statistical Optimization and Its Application for Pentyl Valerate Synthesis.
Applied Biochemistry and Biotechnology ( IF 3 ) Pub Date : 2019-12-10 , DOI: 10.1007/s12010-019-03180-1
Atefeh Ameri 1 , Mojtaba Shakibaie 1, 2 , Mehdi Khoobi 3 , Mohammad Ali Faramarzi 4 , Alieh Ameri 5 , Hamid Forootanfar 2, 6
Affiliation  

Synthesis of (3-aminopropyl) triethoxysilane (APTES)-functionalized graphene oxide (GO) nanosheets, statistical optimization of conditions for immobilization of Bacillus atrophaeus lipase (BaL) on as-synthesized support, and application of the immobilized BaL for esterification of valeric acid were carried out in this investigation. The optimum specific activity of the immobilized BaL (81.60 ± 0.28 U mg−1) was achieved at 3 mg mL−1 of GO-NH2, 50 mM of phosphate buffer, pH 7.0, 60 min sonication time, 100 mM glutaraldehyde, 25 U mL−1 of enzyme, and 8 h immobilization time at 4 °C. The immobilized BaL retained about 90% of its initial activity after 10 days of storage. Moreover, about 70% of the initial activity of the immobilized BaL was retained after 10 cycles of application. The results of esterification studies exhibited that maximum pentyl valerate synthesis using the free BaL (34.5%) and the immobilized BaL (92.7%) occurred in the organic solvent medium (xylene) after 48 h of incubation at 60 °C.



中文翻译:

嗜热芽孢杆菌FSHM2嗜热亲脂酶在胺修饰的氧化石墨烯纳米结构上的固定化:统计优化及其在戊酸戊酯合成中的应用。

(3-氨基丙基)三乙氧基硅烷(APTES)-功能化的氧化石墨烯(GO)纳米片的合成,萎缩芽孢杆菌脂肪酶(Ba L)固定在合成载体上的条件的统计优化,以及固定化Ba L在酯化中的应用在该研究中进行了戊酸。固定化的最佳比活性的Ba L(81.60±0.28毫克ü -1)以3mg毫升达到-1 GO-NH的2,磷酸盐缓冲液50mM的,pH为7.0,60分钟超声处理时间,100mM的戊二醛, 25 U mL -1的酶,在4°C下固定8小时。固定BaL在储存10天后保留了其初始活性的90%。而且,在10个施用循环后,固定的Ba L的初始活性的约70%得以保留。酯化研究的结果表明,在60°C孵育48小时后,使用游离Ba L(34.5%)和固定化Ba L(92.7%)的最大戊酸戊酯合成发生在有机溶剂介质(二甲苯)中。

更新日期:2019-12-10
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