Article
Chemistry, Physical
Jose R. Guimaraes, Diego Carballares, Javier Rocha-Martin, Andres R. Alcantara, Paulo W. Tardioli, Roberto Fernandez-Lafuente
Summary: The lipase from Thermomyces lanuginosus (TLL) was immobilized on a methacrylate macroporous resin coated with octadecyl groups for enhanced stability. Covalent immobilization of the enzyme was achieved by activating the support with divinyl sulfone. The use of different blocking agents affected the functional features of the biocatalyst.
Article
Chemistry, Applied
Sara Arana-Pena, Nathalia S. Rios, Diego Carballares, Luciana R. B. Goncalves, Roberto Fernandez-Lafuente
Summary: CALB and CRL showed similar properties under different immobilization conditions, while RML displayed significant changes. The effects of immobilization conditions on substrate activity and stability vary greatly, requiring careful selection based on specific circumstances.
Article
Biochemistry & Molecular Biology
Pedro Abellanas-Perez, Diego Carballares, Javier Rocha-Martin, Roberto Fernandez-Lafuente
Summary: The objective of this study was to analyze the interaction between buffer nature and chemical modification on enzyme stability. The results showed that there was a significant interaction between the chemical modification of the enzyme surfaces and their stabilities in different buffers. Chemical modification can improve enzyme stability in some buffers while having a negative effect in others.
PROCESS BIOCHEMISTRY
(2023)
Article
Biophysics
Hongbo Suo, Moju Li, Renmin Liu, Lili Xu
Summary: In this study, imidazolium-based ionic liquid was successfully grafted to magnetic polydopamine nanoparticles for lipase immobilization. The immobilized lipase showed excellent activity and stability, with increased affinity to substrate. Additionally, the immobilized lipase can be easily separated from the reaction system with a magnet, providing new ideas for further studies in this field.
COLLOIDS AND SURFACES B-BIOINTERFACES
(2021)
Article
Chemistry, Multidisciplinary
Thays N. da Rocha, Diego Carballares, Jose R. Guimaraes, Javier Rocha-Martin, Paulo W. Tardioli, Luciana R. B. Goncalves, Roberto Fernandez-Lafuente
Summary: Lipases A and B from Candida antarctica, Thermomyces lanuginosus, and Candida rugosa were immobilized on different carriers and exhibited different specificity and optimal activities. The stability of the preparations was strongly influenced by the substrate and conditions for residual activity determination, not necessarily corresponding to the optimal temperatures.
SUSTAINABLE CHEMISTRY AND PHARMACY
(2022)
Article
Biochemistry & Molecular Biology
Sara Arana-Pena, Diego Carballares, Roberto Morellon-Sterling, Javier Rocha-Martin, Roberto Fernandez-Lafuente
Summary: This study achieved the coimmobilization of lipases from Rhizomucor miehei and Candida antarctica, successfully immobilizing both enzymes even when one of them cannot be immobilized initially. A special strategy was developed to desorb inactivated enzyme and re-immobilize a fresh sample, allowing for enzyme reuse.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2022)
Article
Chemistry, Physical
Zou Bin, Feng Ting, Yan Yan, Liu Feng, Onyinye Adesanya Idowu, Suo Hongbo
Summary: A novel cross-linked enzyme aggregate was designed and synthesized using lipase surface modification and immobilization techniques. The resulting enzyme aggregate showed higher activity and stability in esterification reactions, and exhibited improved performance in terms of storage and reusability.
CATALYSIS SCIENCE & TECHNOLOGY
(2022)
Article
Chemistry, Physical
Anna Szelwicka, Karol Erfurt, Sebastian Jurczyk, Slawomir Boncel, Anna Chrobok
Summary: This study proposed a highly efficient method of synthesizing n-butyl acrylate via esterification of acrylic acid and n-butanol in the presence of supported ionic liquid phase biocatalyst. By optimizing the reaction conditions, a 99% yield of n-butyl acrylate was achieved within 24 hours. The use of SILP biocatalyst not only enhanced the activity of CALB, but also demonstrated significant stability over multiple runs.
Article
Environmental Sciences
Waqad Ul Mulk, Mansoor Ul Hassan Shah, Syed Nasir Shah, Qi-Jun Zhang, Asim Laeeq Khan, Mahdi Sheikh, Mohammad Younas, Mashallah Rezakazemi
Summary: The main obstacles in adopting solvent-based CO2 capture technology from power plant flue gases at the industrial scale can be overcome using new green and more stable ionic liquids as solvents. In this study, phosphonium chloride-based ILs immobilized on hydrophobic porous supports were tested for CO2 permeability and selectivity, with PTFE support-based SILM performing the best. This research suggests that phosphonium chloride-based ILs could be better solvent candidates for CO2 removal from large volumes of flue gases.
ENVIRONMENTAL RESEARCH
(2023)
Article
Biochemistry & Molecular Biology
Jose R. Guimaraes, Diego Carballares, Paulo W. Tardioli, Javier Rocha-Martin, Roberto Fernandez-Lafuente
Summary: Modifications with different metal phosphates greatly altered the specificity and enantiospecificity of commercial immobilized lipases. However, enzyme stability was not significantly improved.
Review
Biotechnology & Applied Microbiology
Saadiah A. Abdulmalek, Yunjun Yan
Summary: This review discusses the recent developments in carrier materials and techniques for lipase immobilization, as well as the application of immobilized lipase mixtures in biodiesel synthesis. The review emphasizes the advantages and potential of immobilized lipases in biodiesel production, and presents an overview of the economic and environmental evaluation of enzymatic biodiesel production. The review also suggests the potential extension of using mixed and co-immobilized lipases to other enzymes and processes.
BIOFUELS BIOPRODUCTS & BIOREFINING-BIOFPR
(2022)
Article
Biochemical Research Methods
Marco Mangiagalli, Diletta Ami, Marcella de Divitiis, Stefania Brocca, Tiziano Catelani, Antonino Natalello, Marina Lotti
Summary: This study investigates the effects of short-chain alcohols on the functional and structural responses of immobilized enzyme N-435. It is found that the inactivation process is highly dependent on alcohol concentration and occurs through two different mechanisms.
BIOTECHNOLOGY JOURNAL
(2022)
Article
Chemistry, Applied
Yi-Ping Cao, Gao-Ying Zhi, Li Han, Queting Chen, Dong-Hao Zhang
Summary: The design of a new immobilized lipase entrapped in nano-molecular cages improved its performance in biosynthesis, demonstrating higher activity and stability compared to free and adsorbed lipase. The entrapped lipase exhibited excellent activity and reusability in the biosynthesis of benzyl cinnamate, indicating the nano-molecular cages could inhibit denaturation and maintain lipase activity.
Article
Biochemistry & Molecular Biology
Moju Li, Xusheng Dai, Aifeng Li, Qi Qi, Wenhui Wang, Jia Cao, Zhenting Jiang, Renmin Liu, Hongbo Suo, Lili Xu
Summary: In this study, an ionic liquid-modified magnetic metal-organic framework composite was prepared and used as a support for enzyme immobilization. The immobilized enzyme showed higher catalytic activity, thermal stability, and anti-denaturant properties compared to soluble enzymes. The results demonstrated that the ionic liquid-modified Fe3O4@UiO-66-NH2 has great potential for immobilized enzymes.
Article
Chemistry, Multidisciplinary
Shoronia N. Cross, Alexander H. Al-Feghali, Amy Szuchmacher Blum
Summary: This study investigates the interactions between iron oxide nanoparticles (IONPs) and five common biologically relevant buffers. The results show that phosphate and Tris buffers can bind to the surface of IONPs and cause the release of iron into the solution. Minor etching is observed in HEPES and MOPS buffers, while no etching is observed in MES buffer. Therefore, proper buffer selection should be considered when using IONPs.
Article
Public, Environmental & Occupational Health
Antonio Lopez-Gay, Jeroen Spijker, Helen V. S. Cole, Antonio G. Marques, Margarita Triguero-Mas, Isabelle Anguelovski, Marc Mari-Dell'Olmo, Juan A. Modenes, Dolores alamo-Junquera, Fernando Lopez-Gallego, Carme Borrell
Summary: This study investigated the relationship between COVID-19 incidence and sociodemographic factors in Barcelona. The findings showed that areas with higher population density, an aged population structure, a high presence of nursing homes, a higher proportion of people who left their residential areas during lockdown, and a higher proportion of people working in health-related occupations were more likely to have a higher number of COVID-19 cases. On the other hand, COVID-19 incidence was negatively associated with the percentage of residents with post-secondary education and the population born in countries with a high Human Development Index.
JOURNAL OF EPIDEMIOLOGY AND COMMUNITY HEALTH
(2022)
Article
Chemistry, Physical
Guillermo Garcia-Marquina, Reyes Nunez-Franco, Francesca Peccati, Yi Tang, Gonzalo Jimenez-Oses, Fernando Lopez-Gallego
Summary: This study reveals that mutation clusters in the acyltransferase LovD9 can enhance enzyme kinetics and stability, providing a theoretical basis for simvastatin synthesis. By combining rational mutation clusters, we successfully generated the variant LovD-BuCh2 with catalytic efficiency close to LovD9.
Article
Chemistry, Multidisciplinary
Lorena Betancor, Fernando Lopez-Gallego
Summary: This review explores the combination of isolated enzymes and whole cells for chemical biomanufacturing. Both isolated enzymes and whole-cell biocatalysis have their own advantages, which can be synergistically utilized to improve efficiency and sustainability in bioprocesses. Different architectural approaches, such as combining extracellular enzymes and microorganisms, displaying enzymes on whole cell walls, and integrating enzymes and microorganisms into different materials, are presented as available alternatives for tandem enzyme-cell systems' biotransformations.
CURRENT OPINION IN GREEN AND SUSTAINABLE CHEMISTRY
(2022)
Article
Microbiology
Paula Vidal, Monica Martinez-Martinez, Laura Fernandez-Lopez, Sergi Roda, Celia Mendez-Garcia, Olga V. Golyshina, Victor Guallar, Ana I. Pelaez, Manuel Ferrer
Summary: This study identifies enzymes with potential biotechnological interest from the Los Rueldos acid mine drainage (AMD) system. The enzymes, derived from acidophilic bacteria, exhibit high diversity and potential novelty. Some of these enzymes are adapted to acidic conditions and may have potential applications in plastic degradation.
FRONTIERS IN MICROBIOLOGY
(2022)
Article
Chemistry, Multidisciplinary
Sergi Roda, Laura Fernandez-Lopez, Marius Benedens, Alexander Bollinger, Stephan Thies, Julia Schumacher, Cristina Coscolin, Masoud Kazemi, Gerard Santiago, Christoph G. W. Gertzen, Jose L. Gonzalez-Alfonso, Francisco J. Plou, Karl-Erich Jaeger, Sander H. J. Smits, Manuel Ferrer, Victor Guallar
Summary: The development of PluriZyme TR2E2 with efficient transaminase and esterase activities allows for cascade reactions, particularly in the synthesis of crucial intermediates for antidiabetic drugs. The catalytic power of TR2E2 PluriZyme was demonstrated with a set of beta-keto esters, highlighting the potential of such designs for bioinspired cascade reactions.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2022)
Article
Biochemistry & Molecular Biology
Laura Fernandez-Lopez, Sergi Roda, Jose L. Gonzalez-Alfonso, Francisco J. Plou, Victor Guallar, Manuel Ferrer
Summary: In this study, a catalytically efficient artificial protease was designed and easily produced. By modifying an esterase site, a proteolytic site was successfully created. The resulting artificial enzyme exhibited efficient hydrolysis activity under suitable conditions and could be used for one-pot cascade synthesis reactions.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Biochemistry & Molecular Biology
Ruite Xiang, Laura Fernandez-Lopez, Ana Robles-Martin, Manuel Ferrer, Victor Guallar
Summary: Substrate promiscuity is a desirable property that increases the reusability of enzymes, but finding new substrate promiscuous ester hydrolases is challenging. We have developed a method called EP-pred, which can predict promiscuity from sequence alone and successfully identified ten sequences encoding promiscuous esterases.
Article
Biochemistry & Molecular Biology
Javier Santiago-Arcos, Susana Velasco-Lozano, Fernando Lopez-Gallego
Summary: Immobilized multienzyme systems were successfully achieved using a heterofunctional support activated with three different chemical functionalities. The support, based on agarose microbeads activated with aldehyde, amino, and cobalt chelate moieties, enabled fast and irreversible immobilization of enzymes, resulting in enhanced thermostability (up to 21-fold higher) compared to soluble enzymes. Moreover, this trifunctional support efficiently coimmobilized a multienzyme system consisting of alcohol dehydrogenase, reduced nicotinamide adenine dinucleotide (NADH) oxidase, and catalase, exhibiting higher performance than its free counterpart with a total turnover number (TTN) of 1 x 105 during five batch consecutive cycles. This solid material holds promise as a platform for coimmobilizing multienzyme systems with enhanced properties for stepwise biotransformations.
Article
Multidisciplinary Sciences
Katarzyna Swiderek, Susana Velasco-Lozano, Miquel A. Galmes, Ion Olazabal, Haritz Sardon, Fernando Lopez-Gallego, Vicent Moliner
Summary: Biocatalysis plays a crucial role in plastic recycling. However, the understanding of the molecular mechanisms governing the catalytic performance of plastic-degrading enzymes is limited, hindering the development of more efficient enzyme-based technologies. This study investigates the hydrolysis of PET-derived diesters and PET trimers using CALB and provides insights into CALB's regioselectivity. The findings enable selective hydrolysis of BHET and offer potential applications in the valorization of PET by-products.
NATURE COMMUNICATIONS
(2023)
Article
Multidisciplinary Sciences
Alba Ledesma-Fernandez, Susana Velasco-Lozano, Javier Santiago-Arcos, Fernando Lopez-Gallego, Aitziber L. L. Cortajarena
Summary: In this study, a strategy for organizing multienzymatic systems using a protein scaffold based on TRAP domains is presented, showing improved catalytic output. The scaffold allows for enzymes to be arranged in close proximity, triggering substrate channeling effect and efficient cofactor reuse. The TRAP-scaffolding system demonstrates increased specific productivity in the biosynthesis of amino acids and amines, and immobilization of the scaffold on solid supports creates reusable multi-functional biocatalysts. This research highlights the potential of TRAP-scaffolding systems in increasing the efficiency of cell-free biosynthetic pathways.
NATURE COMMUNICATIONS
(2023)
Article
Biochemistry & Molecular Biology
Laura Fernandez-Lopez, Sergi Roda, Ana Robles-Martin, Ruben Munoz-Tafalla, David Almendral, Manuel Ferrer, Victor Guallar
Summary: Lipases have valuable potential for industrial use, but often require engineering modifications for optimal performance. This study improved the lipase activity by mutating its lid domain and swapping it with another lipase's lid domain, demonstrating the importance of lid domains in determining substrate specificity.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Sergio Serrano-Villar, Camilla Tincati, Sajan C. Raju, Johan S. Saenz, Elena Moreno, Rafael Bargiela, Alfonso Cabello-Ubeda, Elena Sendagorta, Alina Kurz, Jose Perez A. Molina, Amparo de Benito, Johannes R. Hov, Laura Fernandez-Lopez, Alfonso Muriel, Rosa del Campo, Santiago Moreno, Marius Troseid, Jana Seifert, Manuel Ferrer
Summary: Human papillomavirus can lead to HSILs in the anogenital area, and the microbiome may play a role. HIV-MSM individuals have a high risk of anal cancer, but current screening methods for HSILs lack specificity. This study found that elevated levels of microbiome-encoded proteins were associated with HSILs, and measuring these biomarkers improved the current strategy of anal cancer screening.
Article
Chemistry, Multidisciplinary
Eleftheria Diamanti, Susana Velasco-Lozano, Daniel Grajales-Hernandez, Alejandro H. Orrego, Desire Di Silvio, Jose Maria Fraile, Fernando Lopez-Gallego
Summary: Self-sufficient heterogeneous biocatalysts (ssHB) are potential candidates for cofactor-dependent enzymes in chemical biomanufacturing. By immobilizing adenylated cofactors on agarose microbeads through reversible covalent bonds formed between the cis-diol of the ribose in the cofactor backbone and boronic acid, the limitations of current ssHBs in high ionic strength conditions are overcome. The functionality and stability of these ssHBs are demonstrated in reductive aminations, and the immobilized enzymes and cofactors can be reused multiple times.
ACS SUSTAINABLE CHEMISTRY & ENGINEERING
(2023)
Article
Chemistry, Multidisciplinary
Laura Fernandez-Lopez, Isabel Cea-Rama, Julia Alvarez-Malmagro, Anna K. Ressmann, Jose L. Gonzalez-Alfonso, Cristina Coscolin, Patrick Shahgaldian, Francisco J. Plou, Jan Modregger, Marcos Pita, Julia Sanz-Aparicio, Manuel Ferrer
Summary: Metal complexes introduced into protein scaffolds can generate versatile biomimetic catalysts with various catalytic properties. In this study, we synthesized and covalently bound a bipyridinyl derivative to the active site of an esterase, resulting in a biomimetic catalyst that exhibits catecholase activity and enantioselective catalytic oxidation of (+)-catechin.
CHEMICAL COMMUNICATIONS
(2023)
