Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site
authors Brandao, LMD; Barbosa, MS; Souza, RL; Pereira, MM; Lima, AS; Soares, CMF
nationality International
journal BIOTECHNOLOGY PROGRESS
author keywords bioimprinting; esterification reaction; fatty acids; lipase activation; molecular docking
keywords BURKHOLDERIA-CEPACIA LIPASE; CANDIDA-RUGOSA LIPASE; INTERFACIAL ACTIVATION; IONIC LIQUIDS; CATALYZED SYNTHESIS; IMMOBILIZED LIPASE; CRYSTAL-STRUCTURE; OPEN CONFORMATION; ESTERIFICATION; PERFORMANCE
abstract Bioimprinting is an easy, sustainable and low-cost technique that promotes a printing of potential substrates on enzyme structure, inducing a more selective and stable conformation. Bioimprinting promotes conformational changes in enzymes, resulting in better catalytic performance. In this work, the effect of bioimprinting ofBurkholderia cepacialipase (BCL) and porcine pancreatic extracts (PPE) with four different fatty acids (lauric acid (C12:0), myristic acid (C14:0), palmitic acid (C16:0), and stearic acid (C18:0)) was investigated. The results demonstrated that the better bioimprinting effect was in BCL with lauric acid in esterification reaction, promoting BCL activation in which relative enzyme activity was 70 times greater than nonimprinted BCL. Bioimprinting results were influenced by the carbon chain length of fatty acids imprinted in the BCL, in which the effects were weaker with the chain increase. Molecular docking was performed to better understand the bioimprinting method. The results of these simulations showed that indeed all fatty acids were imprinted in the active site of BCL. However, lauric acid presented the highest imprinting preference in the active site of BCL, resulting in the highest relative activity. Furthermore, Fourier transform infrared (FTIR) analysis confirmed important variations in secondary structure of bioimprinting BCL with lauric acid, in which there was a reduction in the alpha-helix content and an increase in the beta-sheet content that facilitated substrate access to the active site of BCL and led higher rigidity, resulting in high activity. Bioimprinted BCL with lauric acid showed excellent operational stability in esterification reaction, maintaining its original relative activity after five successive cycles. Thus, the results show that bioimprinting of BCL with lauric acid is a successful strategy due to its high catalytic activity and reusability.
publisher WILEY
issn 8756-7938
isbn 1520-6033
year published 2021
volume 37
issue 1
digital object identifier (doi) 10.1002/btpr.3064
web of science category 9
subject category Biotechnology & Applied Microbiology; Food Science & Technology
unique article identifier WOS:000562902400001
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journal analysis (jcr 2019):
journal impact factor 2.334
5 year journal impact factor 2.223
category normalized journal impact factor percentile 50.513
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