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Microbial lipase: a new approach for a heterogeneous biocatalyst
Preparative Biochemistry & Biotechnology ( IF 2.9 ) Pub Date : 2020-12-14 , DOI: 10.1080/10826068.2020.1855442
Mariana Vendrasco Tacin 1, 2 , Tales A Costa-Silva 3 , Ariela Veloso de Paula 1 , Jose M Palomo 2 , Valéria de Carvalho Santos-Ebinuma 1
Affiliation  

Abstract

Lipases are enzymes employed in several industrial process and their applicability can be increased if these biocatalysts are in the immobilize form. The objective of this work was to study the immobilization of lipase produced by submerged cultivation of Aspergillus sp. by hydrophobic interaction, evaluating its stability and reuse capacity. The immobilization process on octyl-sepharose (C8) and octadecyl-sepabeads (C18) carriers was possible after the removal of oil excess presented in the fermented broth. The results showed that the enzyme was isolated and concentrated in octyl-sepharose with 22% of the initial activity. To increase the amount of enzyme adsorbed on the carrier, 4 immobilization cycles were performed in a row, on the same carrier, with a final immobilization yield of 151.32% and an increase in the specific activity of 136%. The activity test with immobilized lipase showed that the immobilized enzyme maintained 75% of the initial activity after 20 cycles.



中文翻译:

微生物脂肪酶:一种多相生物催化剂的新方法

摘要

脂肪酶是在几个工业过程中使用的酶,如果这些生物催化剂处于固定形式,它们的适用性会增加。这项工作的目的是研究水下培养曲霉产生的脂肪酶的固定化。通过疏水相互作用,评估其稳定性和再利用能力。辛基琼脂糖 (C 8 ) 和十八烷基 sepabeads (C 18在去除发酵液中存在的过量油后,载体是可能的。结果表明,该酶被分离并浓缩在辛基琼脂糖凝胶中,其活性为初始活性的 22%。为增加载体上酶的吸附量,在同一载体上连续进行4个固定循环,最终固定产率为151.32%,比活增加136%。固定化脂肪酶的活性测试表明,固定化酶在20个循环后仍保持初始活性的75%。

更新日期:2020-12-14
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