The characteristics of insoluble softwood substrates affect fungal morphology, secretome composition, and hydrolytic efficiency of enzymes produced by Trichoderma reesei.

作者: Carl J. Houtman , Vera Novy , Vera Novy , Grzegorz Sabat , Daniel Cullen

DOI: 10.1186/S13068-021-01955-5

关键词:

摘要: Background On-site enzyme production using Trichoderma reesei can improve yields and lower the overall cost of lignocellulose saccharification by exploiting fungal gene regulatory mechanism that enables it to continuously adapt secretion substrate used for cultivation. To harness this, interrelation between characteristics response must be understood. However, morphology or expression studies often lack structural chemical characterization. Here, T. QM6a was cultivated on three softwood substrates: northern bleached Kraft pulp (NBSK) lodgepole pine pretreated either dilute-acid-catalyzed steam pretreatment (LP-STEX) mild alkaline oxidation (LP-ALKOX). With different pretreatments similar starting materials, we presented fungus with systematically modified substrates. This allowed elucidation substrate-induced changes in testing secreted enzymes' hydrolytic strength towards same Results Enzyme activity time courses correlated hemicellulose content cellulose accessibility. Specifically, increased amounts side-chain-cleaving hemicellulolytic enzymes protein produced complex substrates (LP-STEX; LP-ALKOX) observed secretome analysis. Confocal laser scanning micrographs showed micromorphology responded accessibility initial culture viscosity. The latter caused surface charge fiber dimensions, likely restricted mass transfer, resulting morphologies fungi stress. Supplementing a basic cellulolytic mixture concentrated supernatant improved efficiencies substrates, where cellulose, xylan, mannan conversion up 27, 45, 2800%, respectively. improvement most pronounced proteins LP-STEX LP-ALKOX those best case, reached state-of-the-art commercial preparation. Conclusion Cultivation cellulase performance suggests adaptation exploited achieve enhanced enzymatic hydrolysis without priori knowledge specific requirements.

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