The aflatoxin B1 (AFB1) adsorption properties of several lignins isolated by the Pepper's method from grassy plants: Helianthus tuberosus (LS-1), Atriplex patula (LS-2), Rhododendron tomentosum (LS-3), Althaea officinalis (LS-4), Lavatera (LS-5), and from wood of spruce Pícea (LS-6) were studied. The adsorption was conducted in vitro in the modeled conditions of the gastrointestinal tract. The correlations between the values of adsorption-desorption and the parameters of surface-porous structure and chemical structure of the lignins were established. The relationships between the adsorption capacity and properties of the lignins led us to the conclusion that chemisorption play the most important role in the strong adsorption of aflatoxin B1. The contribution of the surface physical properties to the process of adsorption of aflotoxin B1 was not significant. It was shown that the sample of lignin isolated from stems of Althaea officinalis, was characterized by the highest value of strong adsorption of aflatoxin B1.
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http://dx.doi.org/10.1016/j.ijbiomac.2019.12.081 | DOI Listing |
Front Fungal Biol
December 2024
Water Systems and Biotechnology Institute, Faculty of Natural Sciences and Technology, Riga Technical University, Riga, Latvia.
The growing demand for novel enzyme producers to meet industrial and environmental needs has driven interest in lignocellulose-degrading fungi. In this study, lignocellulolytic enzyme production capabilities of environmental fungal isolates collected from boreal coniferous and nemoral summer green deciduous forests were investigated, using Congo Red, ABTS, and Azure B as indicators of cellulolytic and ligninolytic enzyme productions. Through qualitative and quantitative assays, the study aimed to identify promising species for lignocellulose-degrading enzyme secretion and assess their potential for biotechnological applications.
View Article and Find Full Text PDFCurr Microbiol
December 2024
Department of Biology, School of Science, King Mongkut's Institute of Technology Ladkrabang (KMITL), Bangkok, 10520, Thailand.
Lignocellulolytic enzymes isolation from mangrove-derived organisms has many industrial advantages due to their efficiency in dealing with extreme and challenging conditions, such as high temperatures and salt concentrations. This study aimed to isolate fungal enzyme producers from mangrove soil in Thailand to produce lignocellulolytic enzymes (carboxymethyl cellulase: CMCase, xylanase, and laccase) and to characterize these enzymes to support industrial applications. Forty-eight fungi were isolated from the mangrove samples, and their enzyme-producing capabilities were assessed using primary and secondary screening methods.
View Article and Find Full Text PDFSci Rep
December 2024
Division of Research, Innovation, and Economic Development (RIED), Tarleton State University, Stephenville, TX, 76402, USA.
Polycyclic aromatic compounds and petroleum hydrocarbons (PHs) are hazardous pollutants and seriously threaten the environment and human health. However, native microbial communities can adapt to these toxic pollutants, utilize these compounds as a carbon source, and eventually evolve to degrade these toxic contaminants. With this in mind, we isolated 26 bacterial strains from various environmental soil samples.
View Article and Find Full Text PDFJ Fungi (Basel)
November 2024
Amity Institute of Microbial Technology, Amity University Uttar Pradesh, Noida 201313, India.
The present study reports the ability of a fungal isolate DY1, obtained from rotten wood, to degrade alkali lignin (AL) and lignocelluloses in an efficient manner. The efficiency of degradation was monitored by measuring the percentage of decolorization and utilizing GC-MS for identifying degradation products at different time intervals (10, 20, 30, and 40 days). The optimal degradation of alkali lignin (AL) was achieved at 0.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Key Laboratory of Science and Technology of Eco-Textile, Ministry of Education, Jiangnan University, Wuxi, Jiangsu 214122, China. Electronic address:
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