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首页> 外文期刊>Bioprocess and Biosystems Engineering >Encapsulation in a sol-gel matrix of lipase from Aspergillus niger obtained by bioconversion of a novel agricultural residue
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Encapsulation in a sol-gel matrix of lipase from Aspergillus niger obtained by bioconversion of a novel agricultural residue

机译：通过新型农业残留物的生物转化获得的黑曲霉脂肪酶的溶胶-凝胶基质中的包封

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摘要

Lipase from Aspergillus niger was obtained from the solid-state fermentation of a novel agroindustrial residue, pumpkin seed flour. The partially purified enzyme was encapsulated in a sol-gel matrix, resulting in an immobilization yield of 71.4 %. The optimum pH levels of the free and encapsulated enzymes were 4.0 and 3.0, respectively. The encapsulated enzyme showed greater thermal stability at temperatures of 45 and 60 ℃ than the free enzyme. The positive influence of the encapsulation process was observed on the thermal stability of the enzyme, since a longer half-life t_(1/2) and lower deactivation constant were obtained with the encapsulated lipase when compared with the free lipase. kinetic parameters were found to follow the Michaelis-Menten equation. The K_m values indicated that the encapsulation process reduced enzyme-substrate affinity and the V_(max) was about 313 % lower than that obtained with the free lipase. The operational stability was investigated, showing 50 % relative activity up to six cycles of reuse at pH 3.0 at 37 ℃. Nevertheless, the production of lipase from agroindustrial residue associated with an efficient immobilization method, which promotes good catalytic properties of the enzyme, makes the process economically viable for future industrial applications.
机译：来自黑曲霉的脂肪酶是从新型农用工业残留物南瓜籽粉的固态发酵中获得的。将部分纯化的酶封装在溶胶-凝胶基质中，固定化率为71.4％。游离和包封的酶的最佳pH值分别为4.0和3.0。包封的酶在45和60℃的温度下显示出比游离酶更高的热稳定性。观察到封装过程对酶的热稳定性的积极影响，因为与游离脂肪酶相比，封装的脂肪酶可获得更长的半衰期t_（1/2）和更低的失活常数。发现动力学参数遵循Michaelis-Menten方程。 K_m值表明包封过程降低了酶-底物亲和力，并且V_（max）比用游离脂肪酶获得的V_（max）低约313％。考察了操作稳定性，结果表明在pH值为3.0的情况下，在37℃下重复使用六个循环，相对活性为50％。然而，与有效的固定方法相关的由农用工业残渣生产脂肪酶，其促进了酶的良好催化性能，使得该方法在经济上对于未来的工业应用是可行的。

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