Next Article in Journal
Sulforaphane Alters β-Naphthoflavone-Induced Changes in Activity and Expression of Drug-Metabolizing Enzymes in Rat Hepatocytes
Next Article in Special Issue
Monitoring the Activity of Immobilized Lipase with Quinizarin Diester Fluoro-Chromogenic Probe
Previous Article in Journal
Effect of Abscisic Acid on Accumulation of Five Active Components in Root of Glycyrrhiza uralensis
Previous Article in Special Issue
An Efficient Approach for Lipase-Catalyzed Synthesis of Retinyl Laurate Nutraceutical by Combining Ultrasound Assistance and Artificial Neural Network Optimization
Article Menu
Issue 11 (November) cover image

Export Article

Open AccessArticle
Molecules 2017, 22(11), 1930; doi:10.3390/molecules22111930

Preparation and Characterization of Cellulose Triacetate as Support for Lecitase Ultra Immobilization

Laboratory of Polymers Recycling, Chemistry Institute, Federal University of Uberlândia, Uberlândia 38408-144, MG, Brazil
Chemical Engineering Faculty, Federal University of Uberlândia, Uberlândia 38408-144, MG, Brazil
Faculty of Integrated Sciences—FACIP, Federal University of Uberlândia, Ituiutaba 38304-402, MG, Brazil
Author to whom correspondence should be addressed.
Received: 25 September 2017 / Revised: 31 October 2017 / Accepted: 6 November 2017 / Published: 16 November 2017
(This article belongs to the Special Issue Lipases and Lipases Modification)
View Full-Text   |   Download PDF [4699 KB, uploaded 16 November 2017]   |  


The use of polymers as supports for enzyme immobilization is a strategy that enables to remove the enzymes from a chemical reaction and improve their efficiency in catalytic processes. In this work, cellulose triacetate (CTA) was used for physical adsorption of phospholipase Lecitase ultra (LU). CTA is more hydrophobic than cellulose, shows good performance in the lipases immobilization being a good candidate for immobilization of phospholipases. We investigated the immobilization of LU in CTA, the stability of the immobilized enzyme (CTA-LU) and the performance of CTA-LU using soybean oil as a substrate. LU was efficiently immobilized in CTA reaching 97.1% in 60 min of contact with an enzymatic activity of 975.8 U·g−1. The CTA-LU system presents good thermal stability, being superior of the free enzyme and increase of the catalytic activity in the whole range of pH values. The difference observed for immobilized enzyme compared to free one occurs because of the interaction between the enzyme and the polymer, which stabilizes the enzyme. The CTA-LU system was used in the transesterification of soybean oil with methanol, with the production of fatty acid methyl esters. The results showed that CTA-LU is a promising system for enzymatic reactions. View Full-Text
Keywords: cellulose triacetate; immobilization; Lecitase ultra; methanolysis; soybean oil cellulose triacetate; immobilization; Lecitase ultra; methanolysis; soybean oil

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Silva, F.B.; Morais Júnior, W.G.; Silva, C.V.; Vieira, A.T.; Batista, A.C.F.; Faria, A.M.; Assunção, R.M.N. Preparation and Characterization of Cellulose Triacetate as Support for Lecitase Ultra Immobilization. Molecules 2017, 22, 1930.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top