DEPOLYMERIZATION OF KRAFT LIGNIN WITH LACCASE AND PEROXIDASE: A REVIEW

Published in Scientific Bulletin. Series F. Biotechnologies, Vol. XXII
Written by Aglaia BURLACU, Florentina ISRAEL-ROMING, Călina Petruța CORNEA

Lignin is a complex aromatic polymer of phenyl propene units non-linear and randomly linked. The main building blocks are p-coumaryl alcohol, coniferyl alcohol and sinapyl alcohol. Lignin is the third most abundant biopolymer on earth and usually accounts for 15-35% of the lignocellulose biomass. The degradation of lignin is extremely difficult due to the complexity of the chemical structure (variable upon the source) and the high molecular weight. Two major types of enzymes involved in the depolymerization of lignin are oxidoreductase: laccase and peroxidase, the main microbial producers being fungi and some bacteria. Due to its highly branched structure, lignin is considered to be the most recalcitrant component of lignocellulose, most of it not being recovered. Therefore, there’s a demand for more effective methods for depolymerization of lignin in order to obtain value-added products. This review underlines the importance of valorization of lignin through enzymatic depolymerization with laccase and peroxidase.

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BURLACU A., ISRAEL-ROMING F., CORNEA C.P. 2018, DEPOLYMERIZATION OF KRAFT LIGNIN WITH LACCASE AND PEROXIDASE: A REVIEW. Scientific Bulletin. Series F. Biotechnologies, Vol. XXII, ISSN 2285-1364, 172-179.


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