This paper evaluates five phenolic compounds as mediators for kenaf pulp biobleaching by laccase. The results have been compared with the treatment using a non-phenolic mediator, 1-hydroxybenzotriole and laccase alone. The influence of the nature of the chemical mediators used on various pulp properties is discussed. In addition to oxidizing lignin, the phenolic radicals formed in the process take part in condensation and grafting reactions in enzymatic stage. After biobleaching sequence (LP), syringaldehyde was shown to be the best phenolic mediator, allowing a delignification of 43% and 72% ISO brightness. These results were similar to the use of laccase alone due to the role as mediators of syringyl units resulting from oxidative lignin degradation. As a novelty, the study was supplemented with thermogravimetric analysis, with emphasis on the crystallinity degree of the cellulose surface and the aim of elucidating the action mechanisms of laccase-mediator systems on fiber.
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http://dx.doi.org/10.1016/j.biortech.2012.12.014 | DOI Listing |
Enzyme Microb Technol
October 2021
State Key Laboratory of Bio-based Materials and Green Papermaking, Qilu University of Technology, Shandong Academy of Sciences, Jinan, 250353, Shandong, PR China; School of Bioengineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan, 250353, Shandong, PR China. Electronic address:
Exploration of feruloyl esterase (FAE) with the resistance to heat and alkali conditions in biobleaching process to improve the separation efficiency of lignocellulose is the key to achieving green papermaking. Herein, we expressed FAEB of C. thermophilum and obtained a thermostable alkaline FAE that can effectively promote the removal of lignin from pulp.
View Article and Find Full Text PDFMolecules
July 2021
Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang 43400, Malaysia.
The present work reports the biobleaching effect on OPEFB pulp upon utilisation of extracellular xylano-pectinolytic enzymes simultaneously yielded from ADI2. The impacts of different doses, retention times, pH, and temperatures required for the pulp biobleaching process were delineated accordingly. Here, the OPEFB pulp was subjected to pre-treatment with xylano-pectinolytic enzymes generated from the same alkalo-thermotolerant isolate that yielded those of higher quality.
View Article and Find Full Text PDFInt J Biol Macromol
December 2020
Laboratory of Microbial Biotechnology, Enzymatic and Biomolecules (LMBEB), Centre of Biotechnology of Sfax, University of Sfax, P.O. Box 1177, Road Sidi Mansour 6 km, Sfax 3018, Tunisia. Electronic address:
A novel xylanase gene xynBCA, encoding a polypeptide of 439 residues (XynBCA), was cloned from Caldicoprobacter algeriensis genome and recombinantly expressed in Escherichia coli BL21(DE3). The amino acid sequence analysis showed that XynBCA belongs to the glycoside hydrolase family 10. The purified recombinant enzyme has a monomeric structure of 52 kDa.
View Article and Find Full Text PDFCarbohydr Res
May 2020
School of Biology and Biological Engineering, South China University of Technology, Guangzhou, Guangdong, 510006, China; Guangdong Provincial Key Laboratory of Fermentation and Enzyme Engineering, Guangzhou, Guangdong, 510006, China. Electronic address:
A novel GH36 α-galactosidase gene (LrAgal36A) from Lichtheimia ramosa was synthesized and highly expressed in Pichia pastoris. The enzyme titer and protein yield for high-density fermentation in a 5 L fermentor were up to 953.6 U mL and 4.
View Article and Find Full Text PDFBioprocess Biosyst Eng
March 2019
Lignocellulose Biotechnology Laboratory, Department of Microbiology, University of Delhi, South Campus, New Delhi, 110021, India.
Production of laccase from Ganoderma lucidum RCK 2011 under solid-state fermentation (SSF) conditions was optimized using response surface methodology, resulting in an approximate eightfold increase compared to that in the unoptimized media. Further, the enzyme produced under SSF as whole fermented substrate (in situ SSF laccase) was found to be more stable than the in vitro enzyme (harvested by downstreaming processing of fermented wheat bran). Interestingly, the biobleaching potentials of both in situ and in vitro SSF laccases were comparable, saving 25% chlorine dioxide for achieving similar pulp brightness as obtained in the pulp treated chemically.
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