The performance of microbial lipase immobilized onto polyolefin supports for hydrolysis of high oleate sunflower oil

Anand, Akash; Weatherley, L.R.

doi:10.1016/j.procbio.2018.01.027

Cited by 31 publications

(13 citation statements)

References 52 publications

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“…13 For this reasons, the use of these biocatalysts is a very promising alternative for developing environmentally friendly processes. 9 In spite of their advantages, the application of lipases is limited due to high cost, denaturation under operational conditions, 14 and difficulty of recovery and reuse. 15 In order to make lipases more attractive economically, some techniques have been used to optimize their performance, such as enzymatic immobilization, 16 protein engineering, 17 and molecular bioimprinting.…”

mentioning

confidence: 99%

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Brandão

Barbosa

Souza

et al. 2020

Biotechnology Progress

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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 of Burkholderia cepacia lipase (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 α-helix content and an increase in the β-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.

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mentioning

confidence: 99%

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Brandão

Barbosa

Souza

et al. 2020

Biotechnology Progress

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“…However, in a more recent study, Arana-Peña et al 90 demonstrated that the enzyme-enzyme interactions in highly loaded supports may modify the enzyme properties by altering individual enzyme molecule features. However, when the right combination of these variables is attained, remarkable results can be achieved; in the last few decades, numerous reports of immobilized lipases from different sources with enhanced solvent stability, 81,82,91 thermostability, 43,83 and degrees of hyperactivation ranging from 300% to 1000% have been published. 80,83,85,92 Lipase immobilization on polypropylene hollow fibers Hydrophobic polypropylene hollow fibers (PPHF), which have been used as separation agents in the food industries and wastewater treatment plants, also possess the surface properties for lipase immobilization.…”

Section: Polypropylene Used As Immobilization Supportmentioning

confidence: 99%

Polypropylene as a selective support for the immobilization of lipolytic enzymes: hyper‐activation, purification and biotechnological applications

Sánchez-Otero

Quintana‐Castro

Rojas-Vázquez

et al. 2021

J of Chemical Tech & Biotech

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Lipases are the versatile biological catalysts used in a wide range of commercial synthetic applications. Microbial lipases have been widely used in the pharmaceutical, food, textile, oleochemical, paper, and bioenergy industries, in the composition of detergents, and in the production of polymers and enantiomerically pure chemical intermediates. Lipases have a unique lid opening mechanism that makes them interesting biocatalysts to catalyze reactions in hydrophobic environments. Water insoluble substrates have also been efficiently transformed by lipases in organic solvents. The use of lipases in industrial processes could be limited by the cost of their production, the difficulties in their recovery and disposal, or by the harsh conditions of some processes that could inactivate or denature the protein. The immobilization of enzymes helps overcome these physical and economical drawbacks, making the catalyst more active, stable, and reusable, resulting in the reduction of costs and of contaminating and harmful byproducts. Polypropylene has unique properties that aid in the activation of the lid opening mechanism and improve the catalytic efficiency of immobilized lipases. The aim of this review is to present an overview of the uses of polypropylene as a support for immobilization of lipolytic enzymes, the study of the immobilization procedure conditions, the characteristics of the immobilized enzymes, and the perspectives of their use in the future as a powerful tool in sustainable industry.

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“…The lamellar structures of mesoporous cuttlebone powder of Sepia officinalis (CBP) also have a large surface area, which is most suitable to entrap more biomolecules on its surface during immobilization [63]. Moreover, the particle size also affects the enzyme immobilization and reaction rates, both of which are influenced by the amount of interfacial area per unit volume [64]. The modified hollow mesoporous silica support (HMSS) exhibits monodisperse, uniform, and spherical morphology with a particle size of 3.8 µm.…”

Section: Criteriamentioning

confidence: 99%

The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method

et al. 2020

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Four major enzymes commonly used in the market are lipases, proteases, amylases, and cellulases. For instance, in both academic and industrial levels, microbial lipases have been well studied for industrial and biotechnological applications compared to others. Immobilization is done to minimize the cost. The improvement of enzyme properties enables the reusability of enzymes and facilitates enzymes used in a continuous process. Immobilized enzymes are enzymes physically confined in a particularly defined region with retention to their catalytic activities. Immobilized enzymes can be used repeatedly compared to free enzymes, which are unable to catalyze reactions continuously in the system. Immobilization also provides a higher pH value and thermal stability for enzymes toward synthesis. The main parameter influencing the immobilization is the support used to immobilize the enzyme. The support should have a large surface area, high rigidity, suitable shape and particle size, reusability, and resistance to microbial attachment, which will enhance the stability of the enzyme. The diffusion of the substrate in the carrier is more favorable on hydrophobic supports instead of hydrophilic supports. The methods used for enzyme immobilization also play a crucial role in immobilization performance. The combination of immobilization methods will increase the binding force between enzymes and the support, thus reducing the leakage of the enzymes from the support. The adsorption of lipase on a hydrophobic support causes the interfacial activation of lipase during immobilization. The adsorption method also causes less or no change in enzyme conformation, especially on the active site of the enzyme. Thus, this method is the most used in the immobilization process for industrial applications.

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The performance of microbial lipase immobilized onto polyolefin supports for hydrolysis of high oleate sunflower oil

Cited by 31 publications

References 52 publications

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Lipase activation by molecular bioimprinting: The role of interactions between fatty acids and enzyme active site

Polypropylene as a selective support for the immobilization of lipolytic enzymes: hyper‐activation, purification and biotechnological applications

The Immobilization of Lipases on Porous Support by Adsorption and Hydrophobic Interaction Method

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