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Biobleaching is an eco-friendly strategy that can reduce costs and pollution in the pulp and paper industry. Herein, an effective biobleaching approach was proposed using a novel multi-enzyme complex. The multi-enzyme complex was constructed based on mini-cellulosome scaffolding protein integrated with laccase (BpLac) and xylanase (BpXyn) from Bacillus pumilus. The influence of different parameters on the multi-enzyme complex assembly was investigated. The multi-enzyme complex performed better than the free enzyme cocktail in softwood sulfite pulp bleaching. Specifically, free enzyme cocktail treatment decreased the kappa number from 12.2 to 9.1 and increased the brightness from 39.79 to 41.57 % ISO. With more phenolics and reducing sugars releases, the multi-enzyme complex treatment further decreased the kappa number to 8.7 and increased the brightness to 42.09 % ISO. The bleaching performance of the multi-enzyme complex could be further improved at 50 °C, pH 7.0, and 6 % pulp consistency. Measurement of the tensile strength, breaking length, and tearing index suggested that the multi-enzyme complex treatment would not damage fibers in the pulp. Moreover, the multi-enzyme complex treatment could reduce the consumption of HO by 40 % in subsequent chemical bleaching. Therefore, utilizing the multi-enzyme complex in biobleaching is a promising way to advance a cleaner papermaking process.
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http://dx.doi.org/10.1016/j.ijbiomac.2024.139048 | DOI Listing |
Int J Biol Macromol
September 2025
Department of Chemical Engineering, Institute of Chemical Technology, Matunga (E), Mumbai, 400019, India. Electronic address:
Integrating multi-enzyme systems within metal-organic frameworks (MOFs) has garnered significant attention in biocatalysis due to their tunable structural properties and ability to enhance enzyme performance in cascade reactions. The unique features of MOFs, such as well-defined pore apertures, tailorable compositions, and high loading capacity, facilitate the design of robust multi-enzyme bio-composites with enhanced recyclability and specificity. This review explores systematic approaches for the compartmentalization and positional co-immobilization of multiple enzymes within MOFs, focusing on two key strategies: (i) layer-by-layer assembly and (ii) pore-engineered compartmentalization.
View Article and Find Full Text PDFAnimals (Basel)
August 2025
Department of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, AB T6G 2P5, Canada.
Using wheat flour milling (WFM) co-products in pig diets may reduce feed cost. Still, energy digestibility is lower for WFM co-products than for feed grains. Inadequate information exists about their fermentation characteristics and the relationship between digestible energy (DE) value and chemical characteristics or in vitro energy digestibility.
View Article and Find Full Text PDFAnimals (Basel)
August 2025
Tropical Feed Resources Research and Development Center (TROFREC), Department of Animal Science, Faculty of Agriculture, Khon Kaen University, Khon Kaen 40002, Thailand.
This study evaluated the effects of replacing SBM with CWYWEP on in vitro rumen fermentation, nutrient degradability, and gas production kinetics. Citric waste was co-fermented with yeast waste and a multi-enzyme complex for 14 days, then sun-dried and pelleted. The final CWYWEP product contained 50.
View Article and Find Full Text PDFPlant J
August 2025
Centre of Plant Structural and Functional Genomics, Institute of Experimental Botany of the Czech Academy of Sciences, Olomouc, Czech Republic.
Plants rely on tight coordination between nuclear, mitochondrial, and chloroplast genomes to form essential multi-enzyme cytonuclear complexes. Whole-genome duplication (WGD) doubles the nuclear genome, potentially disrupting cytonuclear stoichiometry unless organellar genomes respond accordingly. Targeted analyses of chloroplasts and mitochondria enabled us to dissect the extent and mechanisms of adjustments in both organelles immediately after WGD and across generations in Arabidopsis auto- and allopolyploids.
View Article and Find Full Text PDFJ Hazard Mater
August 2025
Key Laboratory of Industrial Biotechnology, Ministry of Education, & School of Biotechnology, Jiangnan University, Wuxi, Jiangsu 214122, China. Electronic address:
The bioprocess of recycling polyethylene terephthalate (PET) has been extensively studied; however, challenges remain due to its process complexity, low enzymatic performance, and high costs. Here, we devised a strategy termed the Integrated Self-Assembling Multi-Enzyme Display Platform (ISA-MEDP) to directly and efficiently degrade postconsumer PET (pc-PET). We developed a novel surface display system for the unconventional and robust yeast Candida tropicalis, enabling FAST-PETase and MHETase to be functionally anchored onto the cell wall.
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