TY - JOUR AU - Jardak, M. AU - Lami, R. AU - Saadaoui, O. AU - Jlidi, H. AU - Stien, D. AU - Aifa, S. AU - Mnif, S. TI - Control of Staphylococcus epidermidis biofilm by surfactins of an endophytic bacterium Bacillus sp. 15 F JF - ENZYME AND MICROBIAL TECHNOLOGY J2 - ENZYME MICROB TECH VL - 180 PY - 2024 SN - 0141-0229 DO - 10.1016/j.enzmictec.2024.110477 UR - https://m2.mtmt.hu/api/publication/35235110 ID - 35235110 N1 - Laboratory of Molecular and Cellular Screening Processes, Centre of Biotechnology of Sfax, University of Sfax, P O Box 1177, Sidi Mansour Road, Sfax, 3018, Tunisia Sorbonne Université, CNRS, Laboratoire de Biodiversité et Biotechnologies Microbiennes (LBBM), Banyuls-sur-Mer, 66650, France Export Date: 9 September 2024 CODEN: EMTED Correspondence Address: Jardak, M.; Laboratory of Molecular and Cellular Screening Processes, P O Box 1177, Sidi Mansour Road, Tunisia; email: marwajardak@gmail.com Chemicals/CAS: acetonitrile, 75-05-8; isoleucine, 7004-09-3, 73-32-5; leucine, 61-90-5, 7005-03-0; polystyrene, 9003-53-6; surfactin, 24730-31-2 AB - The present paper deals with the preparation and annotation of a surfactin(s) derived from a culture of the endophytic bacterium Bacillus 15 F. The LC-MS analysis of the acetonitrile fraction confirmed the presence of surfactins Leu/Ile7 C15, Leu/Ile7 C14 and Leu/Ile7 C13 with [M+H]+ at m/z 1036.6895, 1022.6741 and 1008.6581, respectively. Various concentrations of the surfactin(s) (hereafter referred to as surfactin-15 F) were used to reduce the adhesion of Staphylococcus epidermidis S61, which served as a model for studying antibiofilm activity on polystyrene surfaces. Incubation of Staphylococcus epidermidis S61 with 62.5 µg/ml of surfactin-15 F resulted in almost complete inhibition of biofilm formation (90.3 ± 3.33 %), and a significant reduction of cell viability (resazurin-based fluorescence was more than 200 times lower). The antiadhesive effect of surfactin-15 F was confirmed by scanning electron microscopy. Surfactin-15 F demonstrated an eradication effect against preformed biofilm, causing severe disruption of Staphylococcus epidermidis S61 biofilm structure and reducing viability. The results suggest that surfactins produced by endophytic bacteria could be an alternative to synthetic products. Surfactin-15 F, used in wound dressings, demonstrated an efficient treatment of the preformed Staphylococcus epidermidis S61 biofilm, and thus having a great potential in medical applications. © 2024 Elsevier Inc. LA - English DB - MTMT ER - TY - JOUR AU - Wang, Yuguang AU - Wu, Mengjing AU - Zheng, Huifang AU - Wu, Dongmei AU - Yao, Panpan AU - Li, Wenjing AU - Jin, Kexin AU - Yu, Xinjun TI - Biomanufacture of L-homoserine lactone building block: A strategy for preparing γ-substituted L-amino acids by modular reaction JF - ENZYME AND MICROBIAL TECHNOLOGY J2 - ENZYME MICROB TECH VL - 176 PY - 2024 PG - 13 SN - 0141-0229 DO - 10.1016/j.enzmictec.2024.110411 UR - https://m2.mtmt.hu/api/publication/34962814 ID - 34962814 LA - English DB - MTMT ER - TY - JOUR AU - Zheng, JM AU - Sun, RB AU - Wu, D AU - Chen, PC AU - Zheng, P TI - Engineered Zea mays phenylalanine ammonia-lyase for improve the catalytic efficiency of biosynthesis trans-cinnamic acid and p-coumaric acid JF - ENZYME AND MICROBIAL TECHNOLOGY J2 - ENZYME MICROB TECH VL - 176 PY - 2024 SN - 0141-0229 DO - 10.1016/j.enzmictec.2024.110423 UR - https://m2.mtmt.hu/api/publication/34878517 ID - 34878517 N1 - Times Cited in Web of Science Core Collection: 0 Total Times Cited: 0 Cited Reference Count: 36; AB - Phenylalanine ammonia-lyase (PAL) plays a pivotal role in the biosynthesis of phenylalanine. PAL from Zea mays (ZmPAL2) exhibits a bi-function of direct deamination of L-phenylalanine (L-Phe) or L-tyrosine(-L-Tyr) to form trans-cinnamic acid or p-coumaric acid. trans-Cinnamic acid and p-coumaric acid are mainly used in flavors and fragrances, food additives, pharmaceutical and other fields. Here, the Activity of ZmPAL2 toward L-Phe or L -Tyr was improved by using semi-rational and rational designs. The catalytic efficiency (kcat/Km) of mutant PT10 (V258I/I459V/Q484N) against L-Phe was 30.8 mu M-1 s-1, a 4.5-fold increase compared to the parent, and the catalytic efficiency of mutant PA1 (F135H/I459L) to L-tyrosine exhibited 8.6 mu M-1 s-1, which was 1.6-fold of the parent. The yield of trans-cinnamic acid in PT10 reached 30.75 g/L with a conversion rate of 98%. Meanwhile, PA1 converted L -Tyr to yield 3.12 g/L of p-coumaric acid with a conversion rate of 95%. Suggesting these two engineered ZmPAL2 to be valuable biocatalysts for the synthesis of trans-cinnamic acid and p-coumaric acid. In addition, MD simulations revealed that the underlying mechanisms of the increased catalytic efficiency of both mutant PT10 and PA1 are attributed to the substrate remaining stable within the pocket and closer to the catalytically active site. This also provides a new perspective on engineered PAL. LA - English DB - MTMT ER - TY - JOUR AU - Xu, Xinqi AU - Chen, Tianheng AU - Xu, Lian AU - Lin, Juan TI - Immobilization of laccase on magnetic nanoparticles for enhanced polymerization of phenols JF - ENZYME AND MICROBIAL TECHNOLOGY J2 - ENZYME MICROB TECH VL - 172 PY - 2024 PG - 9 SN - 0141-0229 DO - 10.1016/j.enzmictec.2023.110331 UR - https://m2.mtmt.hu/api/publication/34672255 ID - 34672255 LA - English DB - MTMT ER - TY - JOUR AU - Alipourfard, Iraj AU - Darvishi, Mohammad AU - Khalighfard, Arghavan AU - Ghazi, Farhood AU - Mobed, Ahmad TI - Nanomaterial-based methods for sepsis management JF - ENZYME AND MICROBIAL TECHNOLOGY J2 - ENZYME MICROB TECH VL - 174 PY - 2024 PG - 11 SN - 0141-0229 DO - 10.1016/j.enzmictec.2023.110380 UR - https://m2.mtmt.hu/api/publication/34639797 ID - 34639797 LA - English DB - MTMT ER - TY - JOUR AU - Liu, Enshi AU - Mercado, Martha Ines Velez AU - Segato, Fernando AU - Wilkins, Mark R. TI - A green pathway for lignin valorization: Enzymatic lignin depolymerization in biocompatible ionic liquids and deep eutectic solvents JF - ENZYME AND MICROBIAL TECHNOLOGY J2 - ENZYME MICROB TECH VL - 174 PY - 2024 PG - 14 SN - 0141-0229 DO - 10.1016/j.enzmictec.2023.110392 UR - https://m2.mtmt.hu/api/publication/34637693 ID - 34637693 LA - English DB - MTMT ER - TY - JOUR AU - Ahmadi, Shabnam AU - Rezaee, Abbas TI - Environmental pollution removal using electrostimulation of microorganisms by alternative current JF - ENZYME AND MICROBIAL TECHNOLOGY J2 - ENZYME MICROB TECH VL - 174 PY - 2024 PG - 8 SN - 0141-0229 DO - 10.1016/j.enzmictec.2023.110369 UR - https://m2.mtmt.hu/api/publication/34623639 ID - 34623639 LA - English DB - MTMT ER - TY - JOUR AU - Manso, Julen Ordenana AU - Nielsen, Martin B. AU - Moya, Eva Balaguer AU - Sandri, Juliana P. AU - Yamakawa, Celina K. AU - Mussatto, Solange I. TI - Intensification of corn fiber saccharification using a tailor made enzymatic cocktail JF - ENZYME AND MICROBIAL TECHNOLOGY J2 - ENZYME MICROB TECH VL - 172 PY - 2024 PG - 6 SN - 0141-0229 DO - 10.1016/j.enzmictec.2023.110347 UR - https://m2.mtmt.hu/api/publication/34609019 ID - 34609019 N1 - Funding Agency and Grant Number: Novo Nordisk Foundation (NNF) , Denmark [NNF20SA0066233] Funding text: This work was supported by the Novo Nordisk Foundation (NNF) , Denmark, grant number: NNF20SA0066233. The authors thank Ingre-dion (Brazil) and Novozymes (Denmark) for kindly providing the corn fiber and the enzyme Cellic (R) CTec2, respectively. AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Chen, Shuai AU - Liu, Jia AU - Gao, Ge AU - Li, Mingchang AU - Cao, Lu AU - Liu, Tongtong AU - Li, Guoqiang AU - Ma, Ting TI - An NAD plus -dependent group III alcohol dehydrogenase involved in long-chain alkane degradation in Acinetobacter venetianus RAG-1 JF - ENZYME AND MICROBIAL TECHNOLOGY J2 - ENZYME MICROB TECH VL - 172 PY - 2024 PG - 10 SN - 0141-0229 DO - 10.1016/j.enzmictec.2023.110343 UR - https://m2.mtmt.hu/api/publication/34604130 ID - 34604130 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Erkanli, M. E. AU - El-Halabi, K. AU - Kim, J.R. TI - Exploring the diversity of β-glucosidase: Classification, catalytic mechanism, molecular characteristics, kinetic models, and applications JF - ENZYME AND MICROBIAL TECHNOLOGY J2 - ENZYME MICROB TECH VL - 173 PY - 2024 SN - 0141-0229 DO - 10.1016/j.enzmictec.2023.110363 UR - https://m2.mtmt.hu/api/publication/34487793 ID - 34487793 N1 - Export Date: 09 January 2024; Cited By: 0; Correspondence Address: J.R. Kim; Department of Chemical and Biomolecular Engineering, New York University, Brooklyn, 6 MetroTech Center, 11201, United States; email: jin.kim@nyu.edu; CODEN: EMTED AB - 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. LA - English DB - MTMT ER -