02073nas a2200265   4500008004100000022001400041245015300055210006900208260000800277300001100285490000800296520117000304653001201474653001101486653001401497653001601511653001401527100002301541700002701564700001801591700003101609700001801640700002601658856012301684       2022                        eng d  a0960-852400aLignocellulose degradation by Penicillium janthinellum enzymes is influenced by its variable secretome and a unique set of feedstock characteristics0 aLignocellulose degradation by Penicillium janthinellum enzymes i  cDEC  a1281290 v3653 a<p>
	Substrate characteristics and proteins that affect lignocellulose-hydrolysis by the hypercellulolytic fungus Peni-cillium janthinellum NCIM 1366 (PJ-1366) were investigated. The hydrolysis rate of PJ-1366 enzymes was very high, with upto 75 % of the reaction being completed in initial 4 h. Comparison of the hydrolytic efficiencies on differently pretreated biomass indicated that the greatest (negative) effect was imparted by lignin, suggesting that improving ligninase activity of the PJ-1366 enzymes may help to improve hydrolysis. Larger pore sizes and higher crystallinity of substrates, which favor enzyme penetration and processive hydrolysis, positively influ-enced hydrolysis efficiency. For alkali-pretreated substrates, 16 FPU/g of PJ-1366 cellulases released the sugar -equivalent of using 10 FPU/g of a commercial biomass hydrolyzing enzyme. By correlation analysis, 41 proteins, including 20 CAZymes were identified, whose abundance in the secretome positively correlated with the cellulase activities of the culture filtrate. These proteins may be considered as the primary drivers of FPase/ CMCase/pNPGase/xylanase activity in PJ-1366.</p>
10aBiofuel10aCAZyme10aCellulase10aPenicillium10aSecretome1 aChristopher, Meera1 aSreeja-Raju, Athiraraj1 aSankar, Meena1 aGokhale, Digambar, Vitthal1 aPandey, Ashok1 aSukumaran, Rajeev, K.  uhttps://library.ncl.res.in/content/lignocellulose-degradation-penicillium-janthinellum-enzymes-influenced-its-variable02489nas a2200265   4500008004100000022001400041245019300055210006900248260000800317300001000325490000700335520152800342653001401870653001201884653001601896653001501912653001401927653001401941100002301955700002701978700003102005700003102036700002602067856013002093       2023                        eng d  a1939-123400aCellulase hyper-producing fungus penicillium janthinellum NCIM 1366 elaborates a wider array of proteins involved in transport and secretion, potentially enabling a diverse substrate range0 aCellulase hyperproducing fungus penicillium janthinellum NCIM 13  cMAR  a61-730 v163 a<p>
	The efficient breakdown of lignocellulose requires the concerted activity of multiple enzymes. Previous studies on Penicillium janthinellum NCIM 1366 (PJ-1366) have revealed a more versatile repertoire of cellulases as compared to the hypercellulolytic strain Trichoderma reesei RUT-C30. Since a robust transport and secretion network is necessary to achieve proficient enzyme production, the transporters and extracellular proteins of PJ-1366 identified from its genome data were compared with those of Penicillium rolfsii (the phylogenetically closest species) and T. reesei RUT-C30 (the industrial work horse for cellulase production). Transmembrane proteins formed 20.4%, 21.0% and 18.2%, respectively of the proteome of PJ-1366, P. rolfsii and T. reesei RUT-C30, and 292 of them were mapped as transporters in PJ-1366. Major facilitator superfamily transporters (264) and sugar transporters (167) are abundant in PJ-1366, which probably aid in the uptake of oligosaccharide inducers of cellulase. The number of extracellular proteins (1007) in PJ-1366 is the highest reported for a Penicillium species. Also, PJ-1366 encoded 1.5 x more proteins involved in carbohydrate metabolism than the other fungi, and its secreted CAZymes belonged to much more diverse families (73), potentially enabling the fungus to act on heterogenous substrates. Structural differences in some untranslated protein response (UPR) effectors like Pdi and Clx detected in PJ-1366 may facilitate unique modes of cellulase regulation.</p>
10aCellulase10aPathway10aPenicillium10aregulation10aSecretion10aTransport1 aChristopher, Meera1 aSreeja-Raju, Athiraraj1 aKooloth-Valappil, Prajeesh1 aGokhale, Digambar, Vitthal1 aSukumaran, Rajeev, K.  uhttps://library.ncl.res.in/content/cellulase-hyper-producing-fungus-penicillium-janthinellum-ncim-1366-elaborates-wider-array