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Isoenzyme characterization of proteases and amylases and partial purification of proteases from filamentous fungi causing biodeterioration of industrial paper
Authors:Jorge Alejandro Rojas  Carlos Cruz  José Fernando Mikán  Luz Stella Villalba  María Caridad Cepero de García  Silvia Restrepo
Institution:1. State Key Laboratory Breeding Base of Marine Genetic Resource, Third Institute of Oceanography, SOA, Xiamen 361005, China;2. South China Sea Bio-Resource Exploitation and Utilization Collaborative Innovation Center, Guangzhou 510000, China;1. Key Laboratory of Northwest Water Resource, Environment and Ecology, MOE, Xi''an University of Architecture and Technology, Xi''an 710055, China;2. Shaanxi Key Laboratory of Environmental Engineering, Xi''an University of Architecture and Technology, Xi''an 710055, China;3. School of Municipal and Environmental Engineering, Jilin Jianzhu University, Changchun 130118, China
Abstract:Biodeterioration is an undesirable process that can affect cultural heritage and economically important materials. Although several biotic and abiotic conditions can accelerate this process, microorganisms are perhaps its main promoters. Fungi are the most important microbial agents of biodeterioration of industrial paper stored in archives. The high genetic plasticity of these organisms allows them to adapt to different environments, using almost any class of materials as substrate. Fungi produce a wide array of enzymes, including cellulases, amylases, and proteases, which are responsible for their gross biodeterioration activity. Thirty-two morphotypes of filamentous fungi were isolated on different media from industrial paper at an advanced stage of biodeterioration. The isolates showed different degrees of cellulolytic, proteolytic, and amylolytic activities on plate assays. The highest proteolytic and amylolytic activities were selected for isoform characterization, which provided an indication of the biochemical diversity that allowed them to colonize these materials. Eladia sacculum was the morphotype selected for partial purification of basic proteases since it has three basic isoforms, simplifying the purification process. We obtained a protein of 35 kDa with a pI of 8.9.
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