Global interest in lignocellulosic biorefineries has increased in the recent past due to technological advancements in sustainable and cost-effective production of numerous commodity and speciality chemicals and fuels from renewable lignocellulosic biomass (LCB). As a result, the market value of biorefinery products has also increased over the time, with an estimated worth of USD 867.7 billion by 2025. However, biorefinery operations, especially enzymatic hydrolysis, suffer from many challenges that limits the cost-effectiveness of conversion of LCB. Therefore, it is essential to understand and address these challenges in future biorefineries. The paper focuses on recent trends and challenges in enzymatic hydrolysis of LCB during lignocellulosic biorefinery operation for greener synthesis of energy, fuels, chemicals and other high-value products. Insights into the gaps in knowledge and technological challenges have also been addressed together with focus on future research needs and perspectives of enzymatic hydrolysis of LCB for biorefinery applications.
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http://dx.doi.org/10.1016/j.biortech.2022.127517 | DOI Listing |
ACS Sustain Resour Manag
January 2025
Department of Agrobiotechnology, IFA-Tulln, Institute of Environmental Biotechnology, BOKU University, Vienna, Konrad-Lorenz-Strasse 20, 3430 Tulln an der Donau, Austria.
Tremendous quantities of textile waste generated and primarily landfilled annually represent a huge risk of contaminating the environment, together with loss of valuable resources. Especially, blended fabrics further pose a challenge for recycling and valorization strategies, while enzymatic hydrolysis offers a highly specific and environmentally friendly solution. In this study, we demonstrate that proteases specifically hydrolyze the wool components in blends with polyester, allowing recovery of pure polyester fibers as well as amino acids and peptides as platform molecules for further valorization.
View Article and Find Full Text PDFFood Chem
January 2025
Department of Grain Science and Industry, Kansas State University, Manhattan, KS 66506, USA. Electronic address:
Food allergens are defined by their stability during digestion, with allergenicity largely influenced by resistance to enzymatic hydrolysis. Ovalbumin (OVA), a major egg protein, is a significant contributor to food allergies, particularly in children. Our previous work demonstrated that high hydrostatic pressure (HHP) treatment reduces OVA allergenicity by disrupting conformational epitopes and altering its structure.
View Article and Find Full Text PDFEnviron Technol
February 2025
Technology Institute, University of Passo Fundo, Passo Fundo, RS, Brazil.
Food waste offers a potential source for bioethanol production, but productivity depends on the chemical composition of the raw materials and the processes involved. However, assessment of the environmental sustainability of these processes is often absent and can be carried out using the Life Cycle Assessment (LCA) methodology. This study aimed to perform an LCA on bioethanol production from mixtures of different wastes, including tubers, fruits, and processed foods, focusing on the gate-to-gate phase.
View Article and Find Full Text PDFPlant Foods Hum Nutr
January 2025
Instituto de Ciencia y Tecnología de Alimentos Córdoba (ICYTAC) - CONICET-UNC, Av. Juan Filloy S/N, Ciudad Universitaria, Córdoba, Argentina.
The focus of this work was to evaluate the differences between the thermal and mechanical effects generated by ultrasound waves on the properties of corn starch, which facilitate the subsequent enzymatic hydrolysis for the generation of porous starches. The results showed that both the thermal and mechanical effects have the capacity to disorganize/alter the structure of starch, impacting on its properties. Characteristics such as particle size, pasting and thermal properties (peak viscosity 1400-1800 cp.
View Article and Find Full Text PDFJ Pharm Sci
January 2025
Faculty of Pharmacy, Kindai University, Osaka 577-8502, Japan.
Acyl glucuronide (AG) is a reactive metabolite that causes idiosyncratic drug toxicity (IDT). Although the instability of AG is used to predict the IDT risk of novel drug candidates, it sometimes overestimates the IDT risk. We investigated whether the rate of enzymatic AG hydrolysis in human liver microsomes (HLM) can predict the risk of IDT.
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