Characterization of Lignocellulolytic Enzymes from White-Rot Fungi Tamilvendan Manavalan • Arulmani Manavalan • Klaus Heese Received: 16 August 2014 / Accepted: 27 October 2014 / Published online: 9 December 2014 Ó Springer Science+Business Media New York 2014 Abstract The development of alternative energy sources by applying lignocellulose-based biofuel technology is critically important because of the depletion of fossil fuel resources, rising fossil fuel prices, security issues regarding the fossil fuel supply, and environmental issues. White-rot fungi have received much attention in recent years for their valuable enzyme systems that effectively degrade ligno- cellulosic biomasses. These fungi have powerful extracel- lular oxidative and hydrolytic enzymes that degrade lignin and cellulose biopolymers, respectively. Lignocellulosic biomasses from either agricultural or forestry wastes are abundant, low-cost feedstock alternatives in nature but require hydrolysis into simple sugars for biofuel produc- tion. This review provides a complete overview of the different lignocellulose biomasses and their chemical compositions. In addition, a complete list of the white-rot fungi-derived lignocellulolytic enzymes that have been identified and their molecular structures, mechanism of action in lignocellulose hydrolysis, and biochemical prop- erties is summarized in detail. These enzymes include ligninolytic enzymes (laccase, manganese peroxidase, lig- nin peroxidase, and versatile peroxidase) and cellulolytic enzymes (endo-glucanase, cellobiohydrolase, and beta- glucosidase). The use of these fungi for low-cost ligno- cellulolytic enzyme production might be attractive for biofuel production. Abbreviations AAO Aryl-alcohol oxidase BGL Beta-glucosidase CMC Carboxy methyl cellulose CMCase Carboxymethyl cellulase Cpd-I Compound I Cpd-II Compound I DTT Dithiothreitol EG Endo-glucanase CBH Cellobiohydrolase CBQ Cellobiose:quinone oxidoreductase CDH Cellobiose dehydrogenase FDH NAD-dependent formate dehydrogenase GLO Glyoxal oxidase LiP Lignin peroxidase MnP Manganese peroxidase ODC Oxalate decarboxylase pI Isoelectric point pNPC p-Nitrophenyl-beta-D-cellobioside pNPG para-Nitrophenyl beta-D-glucopyranoside pNPL p-Nitrophenyl-beta-D-lactoside SDS-PAGE Sodium dodecyl sulfate polyacrylamide gel electrophoresis VA Veratryl alcohol VP Versatile peroxidase Electronic supplementary material The online version of this article (doi:10.1007/s00284-014-0743-0) contains supplementary material, which is available to authorized users. T. Manavalan Centre for Advanced Studies in Botany, University of Madras, Chennai 600 025, Tamil Nadu, India A. Manavalan Department of Clinical Medicine - Stereology, Aarhus University, Wilhelm Meyers Alle ´ 3, 8000 Aarhus C, Denmark K. Heese (&) Graduate School of Biomedical Science and Engineering, Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul 133-791, Republic of Korea e-mail: klaus.heese@rub.de; klaus@hanyang.ac.kr 123 Curr Microbiol (2015) 70:485–498 DOI 10.1007/s00284-014-0743-0