Abstract
Trichoderma reesei is a mesophilic, filamentous fungus, and it is a major industrial source of cellulases, but its lignocellulolytic protein expressions on lignocellulosic biomass are poorly explored at present. The extracellular proteins secreted by T. reesei QM6a wild-type and hypercellulolytic mutant Rut C30 grown on natural lignocellulosic biomasses were explored using a quantitative proteomic approach with 8-plex high throughput isobaric tags for relative and absolute quantification (iTRAQ) and analyzed by liquid chromatography tandem mass spectrometry. We quantified 230 extracellular proteins, including cellulases, hemicellulases, lignin-degrading enzymes, proteases, protein-translocating transporter, and hypothetical proteins. Quantitative iTRAQ results suggested that the expressions and regulations of these lignocellulolytic proteins in the secretome of T. reesei wild-type and mutant Rut C30 were dependent on both nature and complexity of different lignocellulosic carbon sources. Therefore, we discuss here the essential lignocellulolytic proteins for designing an enzyme mixture for optimal lignocellulosic biomass hydrolysis.
Highlights
Lignocellulose, a major component of plant biomass produced by photosynthesis, is abundant, renewable, and sustainable; it is no surprise that lignocellulosic bioenergy has become an intense subject of investigation
Functional Classification of Extracellular Proteins—Our analysis focused on the secretome of T. reesei QM6a and mutant Rut C30 in cellulose and natural lignocellulosic biomass culture conditions using isobaric tags for relative and absolute quantitation (iTRAQ) labeling
Little work has been done on the proteomic analysis of secretome by T. reesei using lignocellulosic biomasses as major carbon sources
Summary
Lignocellulose, a major component of plant biomass produced by photosynthesis, is abundant, renewable, and sustainable; it is no surprise that lignocellulosic bioenergy has become an intense subject of investigation now. To date, optimized cultivation conditions, operational parameters, genetic mutation, and manipulation have been developed to enhance enzyme production potential [10] Morphological features, such as pellets, mycelial aggregates, and freely dispersed mycelia have been correlated to enzyme productions [11, 12]. To enhance enzyme production potential, enzyme-inducing substrates such as cellobiose [17], lactose [18], sophorose [19], and cellulose [20, 21] were tested Despite these efforts, required breakthrough in an economical enzyme production to further its application in lignocellulosic biofuel have not yet been achieved. The expression level of the secreted proteins by T. reesei QM6a and Rut C30 and their mechanistic role and the essential proteins required for in vitro reconstitution of enzyme mixture for lignocellulosic biomass were discussed
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