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Effective management and the valorization of agro-industrial lignocellulosic feedstocks can only be realized if a versatile cellulase cocktail is developed that can release glucose at affordable cost irrespective of biomass type. In the present study the flexibility of using cellulase cocktail obtained from mutant UV-8 of Talaromyces verruculosus IIPC 324 in depolymerizing multiple agro-industrial lignocellulosic feedstocks was explored. Five different dilute acid pretreated biomasses were evaluated and cellulase loading was done at 25 mg protein/g cellulose content. After 72 h of hydrolysis at 55 °C and pH 4.5, corn cob and rice straw emerged as the easiest and toughest substrates with saccharification yield of 83.9 ± 1.17 and 35.5 ± 1.16% respectively from their cellulose fraction. Addition of PEG 6000 could retain >65% of all mono-component enzymes present in cellulase cocktail. Structural elucidation of biomasses gave an insight about key features responsible for variable recalcitrance in the different agro-industrial feedstock. Cellulose hydrolysis showed a significant negative correlation in the order of Cr I > S/G ratio > ash content. The chemical composition of lignin had a major impact on enzyme-lignin interactions. Higher H lignin content and lower S/G ratio promoted enzyme desorption, thereby increasing the likelihood of their recycling and reuse.
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http://dx.doi.org/10.1016/j.ijbiomac.2020.03.133 | DOI Listing |
Int J Biol Macromol
September 2025
Protein Research Department, Genetic Engineering and Biotechnology Research Institute (GEBRI), City of Scientific Research and Technological Applications (SRTA-City), New Borg El-Arab, Alexandria, 21934, Egypt. Electronic address:
The growing demand for sustainable agriculture imposes innovative biocontrol strategies to mitigate phytopathogen threats while reducing dependence on chemical pesticides. This review explores the current knowledge on enzyme-based biocontrol, focusing on hydrolytic enzymes (e.g.
View Article and Find Full Text PDFBiotechnol J
September 2025
Guangdong Key Laboratory of Fermentation and Enzyme Engineering, School of Biology and Biological Engineering , South China University of Technology, Guangzhou, P. R. China.
Ramie fiber, an exceptional natural textile material, requires degumming treatment to obtain spinnable mature fibers. Pectate lyase stands as the most effective enzyme for degumming by specifically removing pectin that binds multiple gummy components. However, commercial enzyme cocktails often contain cellulase activities causing significant fiber damage.
View Article and Find Full Text PDFBioengineered
December 2025
Department of Biotechnology, University of Inland Norway, Hamar, Norway.
Spent mushroom substrate (SMS), the main by-product of mushroom cultivation, is a source of sugars that can be released by saccharification. This work aimed at investigating the enzymatic saccharification of the polysaccharides of the SMS of shiitake () and oyster mushroom () and exploring the lignin extraction from the saccharification residues. First, analytical enzymatic saccharification (AES) with a cellulase cocktail and an experimental hemicellulase-rich preparation was applied.
View Article and Find Full Text PDFWorld J Microbiol Biotechnol
July 2025
Department of Microbiology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India.
GH7 cellobiohydrolases (CBH1s) are essential for depolymerizing crystalline cellulose, yet the hypercellulolytic thermophile Rasamsonia emersonii secretes them only in low amounts, leaving a gap in its native enzyme cocktail. To see whether a cognate CBH1 could fill this gap and how it stacks up against the industrial workhorse strain Trichoderma reesei Cel7A, we codon optimized the R. emersonii gene (Rem_GH7CBHI), expressed it in Pichia pastoris and purified the recombinant enzyme for structural and functional analysis.
View Article and Find Full Text PDFEnzyme Microb Technol
October 2025
Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe, Hyogo 657-8501, Japan. Electronic address:
Aspergillus oryzae is a filamentous fungus that possesses various types of carbohydrate -degrading enzymes. Among these, isoprimeverose-producing enzyme (IpeA), acts on a key component of the plant cell wall structure, xyloglucan, to catalyze the release of isoprimeverose - a rare disaccharide that is expected to possess valuable prebiotics properties. Despite these expectations, however, a process for the effective production of isoprimeverose from the xyloglucan still requires further development for commercial-level application.
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