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CALB固定于活化壳聚糖上：在超临界和近临界二氧化碳中的酶促合成应用。

Immobilization of CALB on activated chitosan: Application to enzymatic synthesis in supercritical and near-critical carbon dioxide.

作者信息

Dos Santos José C S, Bonazza Horacio L, de Matos Leonardo J B L, Carneiro Elizabete A, Barbosa Oveimar, Fernandez-Lafuente Roberto, Gonçalves Luciana R B, de Sant' Ana Hosiberto B, Santiago-Aguiar Rílvia S

机构信息

Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, CEP 62785-000, Acarape, CE, Brazil.

Instituto de Desarrollo Tecnológico para la Industria Química, Paraje "El Pozo", RN 168, km 0, Santa Fe, 3000, Argentina.

出版信息

Biotechnol Rep (Amst). 2017 Feb 28;14:16-26. doi: 10.1016/j.btre.2017.02.003. eCollection 2017 Mar.

DOI:10.1016/j.btre.2017.02.003
PMID:28459004
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5397107/
Abstract

The objective of this new paper was to evaluate the enzymatic esterification reaction conducted in supercritical or near-critical CO, catalyzed by immobilized lipase B from (CALB). The biocatalyst was prepared through the immobilization of CALB by covalent attachment using chitosan sequentially activated with Glycidol, ethylenediamine (EDA) and glutaraldehyde as support. In order to determine the best operational conditions of the esterification reaction (1: 1 (alcohol-acid); biocatalyst content, 10% (by substrate mass); 45 °C), an experimental design (2) was conducted to evaluate the effects of the following parameters: alcohol to oil molar ratios, reaction time and temperature. The maximum loading of chitosan was 20 mg protein/g support, and the thermal and solvent stability of the new biocatalyst was higher than that of the CALB-GX (by a 26-fold factor), CALB-OC (by a 53-fold factor) and Novozym 435 (by a 3-fold factor). The maximum conversion was 46.9% at a temperature of 29.9 °C, ethanol to oleic acid molar ratio equal to 4.50:1, and a reaction time of 6.5 h. Additionally, the removal of water from the medium, by using molecular sieves, promoted a 16.0% increase in the conversion of oleic acid into ethyl esters.

摘要

这篇新论文的目的是评估在超临界或近临界二氧化碳中由南极假丝酵母脂肪酶B（CALB）催化的酶促酯化反应。通过使用依次用缩水甘油、乙二胺（EDA）和戊二醛活化的壳聚糖作为载体，通过共价连接固定CALB来制备生物催化剂。为了确定酯化反应的最佳操作条件（1:1（醇-酸）；生物催化剂含量，10%（基于底物质量）；45℃），进行了一项实验设计（2）以评估以下参数的影响：醇与油的摩尔比、反应时间和温度。壳聚糖的最大负载量为20mg蛋白质/g载体，新型生物催化剂的热稳定性和溶剂稳定性高于CALB-GX（高2倍）、CALB-OC（高53倍）和诺维信435（高3倍）。在温度为29.9℃、乙醇与油酸摩尔比等于4.50:1、反应时间为6.5小时时，最大转化率为46.9%。此外，通过使用分子筛从介质中除去水，使油酸转化为乙酯的转化率提高了16.0%。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/14ba43260485/gr9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/0908f77ce622/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/9e0fae5cbb3e/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/3a8b3407b641/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/15e67438bdf5/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/e3511d7cb882/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/88090a55ab5c/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/b1f1c770aba8/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/981b1bdebca5/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/dd0fadd3d683/gr8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/14ba43260485/gr9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/0908f77ce622/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/9e0fae5cbb3e/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/3a8b3407b641/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/15e67438bdf5/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/e3511d7cb882/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/88090a55ab5c/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/b1f1c770aba8/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/981b1bdebca5/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/dd0fadd3d683/gr8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9884/5397107/14ba43260485/gr9.jpg

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