@article{MTMT:34672255, title = {Immobilization of laccase on magnetic nanoparticles for enhanced polymerization of phenols}, url = {https://m2.mtmt.hu/api/publication/34672255}, author = {Xu, Xinqi and Chen, Tianheng and Xu, Lian and Lin, Juan}, doi = {10.1016/j.enzmictec.2023.110331}, journal-iso = {ENZYME MICROB TECH}, journal = {ENZYME AND MICROBIAL TECHNOLOGY}, volume = {172}, unique-id = {34672255}, issn = {0141-0229}, keywords = {magnetic nanoparticle; LACCASE IMMOBILIZATION; Phenol polymerization}, year = {2024}, eissn = {1879-0909}, orcid-numbers = {Xu, Lian/0000-0002-0714-6446} } @article{MTMT:34639797, title = {Nanomaterial-based methods for sepsis management}, url = {https://m2.mtmt.hu/api/publication/34639797}, author = {Alipourfard, Iraj and Darvishi, Mohammad and Khalighfard, Arghavan and Ghazi, Farhood and Mobed, Ahmad}, doi = {10.1016/j.enzmictec.2023.110380}, journal-iso = {ENZYME MICROB TECH}, journal = {ENZYME AND MICROBIAL TECHNOLOGY}, volume = {174}, unique-id = {34639797}, issn = {0141-0229}, keywords = {NANOPARTICLES; Sepsis; biosensors; sepsis management; medical approaches}, year = {2024}, eissn = {1879-0909}, orcid-numbers = {Alipourfard, Iraj/0000-0001-5164-8606; Mobed, Ahmad/0000-0001-8939-3688} } @article{MTMT:34637693, title = {A green pathway for lignin valorization: Enzymatic lignin depolymerization in biocompatible ionic liquids and deep eutectic solvents}, url = {https://m2.mtmt.hu/api/publication/34637693}, author = {Liu, Enshi and Mercado, Martha Ines Velez and Segato, Fernando and Wilkins, Mark R.}, doi = {10.1016/j.enzmictec.2023.110392}, journal-iso = {ENZYME MICROB TECH}, journal = {ENZYME AND MICROBIAL TECHNOLOGY}, volume = {174}, unique-id = {34637693}, issn = {0141-0229}, keywords = {Biorefinery; Lignin fractionation; Biocompatible solvents; Biological lignin conversion; Consolidated lignin valorization}, year = {2024}, eissn = {1879-0909} } @article{MTMT:34623639, title = {Environmental pollution removal using electrostimulation of microorganisms by alternative current}, url = {https://m2.mtmt.hu/api/publication/34623639}, author = {Ahmadi, Shabnam and Rezaee, Abbas}, doi = {10.1016/j.enzmictec.2023.110369}, journal-iso = {ENZYME MICROB TECH}, journal = {ENZYME AND MICROBIAL TECHNOLOGY}, volume = {174}, unique-id = {34623639}, issn = {0141-0229}, keywords = {pollution; electrostimulation; Environment; Bioelectrochemistry; Alternative current}, year = {2024}, eissn = {1879-0909} } @article{MTMT:34609019, title = {Intensification of corn fiber saccharification using a tailor made enzymatic cocktail}, url = {https://m2.mtmt.hu/api/publication/34609019}, author = {Manso, Julen Ordenana and Nielsen, Martin B. and Moya, Eva Balaguer and Sandri, Juliana P. and Yamakawa, Celina K. and Mussatto, Solange I.}, doi = {10.1016/j.enzmictec.2023.110347}, journal-iso = {ENZYME MICROB TECH}, journal = {ENZYME AND MICROBIAL TECHNOLOGY}, volume = {172}, unique-id = {34609019}, issn = {0141-0229}, abstract = {The transition from an economic model based on resource extraction to a more sustainable and circular economy requires the development of innovative methods to unlock the potential of raw materials such as lignocellulosic biomasses. Corn fiber differs from more traditional lignocellulosic biomasses due to its high starch content, which provides additional carbohydrates for fermentation-based biomanufacturing processes. Due to its unique chemical composition, this study focused on the development of a tailor made enzymatic cocktail for corn fiber saccharification into monosaccharides. Three commercially available hydrolytic enzymes (Cellic (R) CTec2, Pentopan (R) Mono BG, and Termamyl (R) 300 L) were combined to hydrolyze the polysaccharide structure of the three main carbohydrate fractions of corn fiber (cellulose, hemicellulose and starch, respectively). Prior to saccharification, corn fiber was submitted to a mild hydrothermal pretreatment (30 min at 100 degrees C). Then, two experimental designs were used to render an enzymatic cocktail capable of providing efficient release of monosaccharides. Using 60 FPU/g DM of Cellic (R) CTec2 and 4.62 U/g DM of Termamyl (R) 300 L, without addition of Pentopan (R) Mono BG, resulted in the highest efficiencies for glucose and xylose release (66% and 30%, respectively). While higher enzyme dosages could enhance the saccharification efficiency, adding more enzymes would have a more pronounced effect on the overall process costs rather than in increasing the efficiency for monosaccharides release. The results revealed that the recalcitrance of corn fiber poses a problem for its full enzymatic degradation. This fact combined with the unique chemical composition of this material, justify the need for developing a tailor made enzymatic cocktail for its degradation. However, attention should also be given to the pretreatment step to reduce even more the recalcitrance of corn fiber and improve the performance of the tailored cocktail, as a consequence.}, keywords = {design of experiments; HEMICELLULASES; Cellulases; enzymatic saccharification; corn fiber}, year = {2024}, eissn = {1879-0909}, orcid-numbers = {Mussatto, Solange I./0000-0002-7182-6198} } @article{MTMT:34604130, title = {An NAD plus -dependent group III alcohol dehydrogenase involved in long-chain alkane degradation in Acinetobacter venetianus RAG-1}, url = {https://m2.mtmt.hu/api/publication/34604130}, author = {Chen, Shuai and Liu, Jia and Gao, Ge and Li, Mingchang and Cao, Lu and Liu, Tongtong and Li, Guoqiang and Ma, Ting}, doi = {10.1016/j.enzmictec.2023.110343}, journal-iso = {ENZYME MICROB TECH}, journal = {ENZYME AND MICROBIAL TECHNOLOGY}, volume = {172}, unique-id = {34604130}, issn = {0141-0229}, abstract = {Alcohol dehydrogenases (ADHs) are a class of key enzymes responsible for the oxidation of alkyl alcohols in the aerobic alkane metabolic pathway. Currently, the degradation mechanisms of short-and medium-chain alkanes are commonly reported, while those of long-chain alkanes have received less attention. In this work, a putative long-chain ADH was screened from Acinetobacter venetianus RAG-1 via RNA-seq with n-octacosane (C28) as the sole carbon source. Conserved sequence analysis revealed that it is a group III (Fe-containing/activated) ADH, which is widespread in the genus Acinetobacter. The deletion of adhA led to a significant reduction in the degradation of C28. AdhA exhibited optimal oxidative activity at pH 8.0 and 50 degrees C with NAD+ as coenzyme, while showing better tolerability to chemical reagents. Enzyme activity assay showed that AdhA owed the oxidative activity to a wide range of substrates including alkyl alcohols (C1-C32) and some isomeric alcohols, such as isopropanol, isobutanol, isoamyl alcohol, and propanetriol, and could reduce the alkyl aldehyde (C1-C12). Meanwhile, the binding of AdhA to different alkyl alcohols was mediated by different amino acids. AdhA is an ADH with an extremely broad substrate utilization range and excellent biochemical characteristics. These results provided important insights in the subsequent investigation of long-chain alkane degradation and petroleum pollution bioremediation.}, keywords = {Acinetobacter venetianus; Long-chain alcohol dehydrogenase; Long-chain alkane degradation}, year = {2024}, eissn = {1879-0909} } @article{MTMT:34487793, title = {Exploring the diversity of β-glucosidase: Classification, catalytic mechanism, molecular characteristics, kinetic models, and applications}, url = {https://m2.mtmt.hu/api/publication/34487793}, author = {Erkanli, M. E. and El-Halabi, K. and Kim, J.R.}, doi = {10.1016/j.enzmictec.2023.110363}, journal-iso = {ENZYME MICROB TECH}, journal = {ENZYME AND MICROBIAL TECHNOLOGY}, volume = {173}, unique-id = {34487793}, issn = {0141-0229}, abstract = {High-value chemicals and energy-related products can be produced from biomass. Biorefinery technology offers a sustainable and cost-effective method for this high-value conversion. β-glucosidase is one of the key enzymes in biorefinery processes, catalyzing the production of glucose from aryl-glycosides and cello-oligosaccharides via the hydrolysis of β-glycosidic bonds. Although β-glucosidase plays a critical catalytic role in the utilization of cellulosic biomass, its efficacy is often limited by substrate or product inhibitions, low thermostability, and/or insufficient catalytic activity. To provide a detailed overview of β-glucosidases and their benefits in certain desired applications, we collected and summarized extensive information from literature and public databases, covering β-glucosidases in different glycosidase hydrolase families and biological kingdoms. These β-glucosidases show differences in amino acid sequence, which are translated into varying degrees of the molecular properties critical in enzymatic applications. This review describes studies on the diversity of β-glucosidases related to the classification, catalytic mechanisms, key molecular characteristics, kinetics models, and applications, and highlights several β-glucosidases displaying high stability, activity, and resistance to glucose inhibition suitable for desired biotechnological applications. © 2023 Elsevier Inc.}, keywords = {Humans; metabolism; CLASSIFICATION; KINETICS; KINETICS; HYDROLYSIS; HYDROLYSIS; human; CATALYSIS; Chemistry; amino acid sequence; amino acid sequence; GLUCOSE; GLUCOSE; GLUCOSE; Substrate Specificity; KINETIC MODELS; HYDROLASES; Glycosides; glycoside; Catalyst activity; kinetic model; Cost effectiveness; beta glucosidase; Kinetic theory; Kinetic parameters; enzyme specificity; Bioconversion; glycosidase; Glycoside Hydrolases; Glycoside Hydrolases; Refining; β-glucosidase; β-glucosidase; Biorefineries; Molecular characteristics; Glycoside hydrolase; beta-Glucosidase; Biorefinery; Glucosidase; Industrial enzymes; Catalytic mechanisms; High-value chemicals; industrial enzyme; Energy related products}, year = {2024}, eissn = {1879-0909} } @article{MTMT:34487042, title = {Comparative analysis of Chrysoporthe cubensis exoproteomes and their specificity for saccharification of sugarcane bagasse}, url = {https://m2.mtmt.hu/api/publication/34487042}, author = {Tavares, Murillo Peterlini and Morgan, Túlio and Gomes, Riziane Ferreira and Mendes, Jean Pierre Rocha and Castro-Borges, William and Maitan-Alfenas, Gabriela Piccolo and Guimarães, Valéria Monteze}, doi = {10.1016/j.enzmictec.2023.110365}, journal-iso = {ENZYME MICROB TECH}, journal = {ENZYME AND MICROBIAL TECHNOLOGY}, volume = {173}, unique-id = {34487042}, issn = {0141-0229}, year = {2024}, eissn = {1879-0909}, pages = {110365} } @article{MTMT:34224562, title = {Comparison of hydrothermolysis and mild-alkaline pretreatment methods on enhancing succinic acid production from hydrolyzed corn fiber}, url = {https://m2.mtmt.hu/api/publication/34224562}, author = {Vallecilla, Yepez L. and Bamaca, Saquic B. and Wilkins, M.R.}, doi = {10.1016/j.enzmictec.2023.110346}, journal-iso = {ENZYME MICROB TECH}, journal = {ENZYME AND MICROBIAL TECHNOLOGY}, volume = {172}, unique-id = {34224562}, issn = {0141-0229}, year = {2024}, eissn = {1879-0909} } @article{MTMT:34373228, title = {Coriolus versicolor laccase-based inorganic protein hybrid synthesis for application in biomass saccharification to enhance biological production of hydrogen and ethanol}, url = {https://m2.mtmt.hu/api/publication/34373228}, author = {Patel, Sanjay K. S. and Gupta, Rahul K. and Kim, In-Won and Lee, Jung-Kul}, doi = {10.1016/j.enzmictec.2023.110301}, journal-iso = {ENZYME MICROB TECH}, journal = {ENZYME AND MICROBIAL TECHNOLOGY}, volume = {170}, unique-id = {34373228}, issn = {0141-0229}, abstract = {In this study, a bio-friendly inorganic protein hybrid-based enzyme immobilization system using partially purified Coriolus versicolor laccase (CvLac) was successfully applied to biomass hydrolysis for the enhancement of sugar production aimed at generating biofuels. After four days of incubation, the maximum CvLac production was achieved at 140 U/mg of total protein in the presence of inducers such as copper and wheat bran after four days of incubation. Crude CvLac immobilized through inorganic protein hybrids such as nanoflowers (NFs) using zinc as Zn-3(PO4)(2)/CvLac hybrid NFs (Zn/CvLac-NFs) showed a maximum encapsulation yield of 93.4% and a relative activity of 265% compared to free laccase. The synthesized Zn/CvLac-NFs exhibited significantly improved activity profiles and stability compared to free enzymes. Furthermore, Zn/CvLac-NFs retained a significantly high residual activity of 96.2% after ten reuse cycles. The saccharification of poplar biomass improved similar to 2-fold in the presence of Zn/CvLac-NFs, with an 8-fold reduction in total phenolics compared to the control. The Zn/CvLac-NFs treated biomass hydrolysate showed high biological hydrogen (H-2) production and ethanol conversion efficiency of up to 2.68 mol/mol of hexose and 79.0% compared to the control values of 1.27 mol of H-2/mol of hexose and 58.4%, respectively. The CvLac hybrid NFs are the first time reported for biomass hydrolysis, and a significant enhancement in the production of hydrogen and ethanol was reported. The synthesis of such NFs based on crude forms of diverse enzymes can potentially be extended to a broad range of biotechnological applications.}, keywords = {STABILITY; LACCASE IMMOBILIZATION; Protein-inorganic hybrid; Biohydrogen, bioethanol}, year = {2023}, eissn = {1879-0909}, orcid-numbers = {Lee, Jung-Kul/0000-0001-7384-5301} }