<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Christopher, Meera</style></author><author><style face="normal" font="default" size="100%">Sreeja-Raju, Athiraraj</style></author><author><style face="normal" font="default" size="100%">Sankar, Meena</style></author><author><style face="normal" font="default" size="100%">Gokhale, Digambar Vitthal</style></author><author><style face="normal" font="default" size="100%">Pandey, Ashok</style></author><author><style face="normal" font="default" size="100%">Sukumaran, Rajeev K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Lignocellulose degradation by Penicillium janthinellum enzymes is influenced by its variable secretome and a unique set of feedstock characteristics</style></title><secondary-title><style face="normal" font="default" size="100%">Bioresource Technology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biofuel</style></keyword><keyword><style  face="normal" font="default" size="100%">CAZyme</style></keyword><keyword><style  face="normal" font="default" size="100%">Cellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">Penicillium</style></keyword><keyword><style  face="normal" font="default" size="100%">Secretome</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">365</style></volume><pages><style face="normal" font="default" size="100%">128129</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	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.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
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	11.889&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Christopher, Meera</style></author><author><style face="normal" font="default" size="100%">Sreeja-Raju, Athiraraj</style></author><author><style face="normal" font="default" size="100%">Kooloth-Valappil, Prajeesh</style></author><author><style face="normal" font="default" size="100%">Gokhale, Digambar Vitthal</style></author><author><style face="normal" font="default" size="100%">Sukumaran, Rajeev K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Cellulase hyper-producing fungus penicillium janthinellum NCIM 1366 elaborates a wider array of proteins involved in transport and secretion, potentially enabling a diverse substrate range</style></title><secondary-title><style face="normal" font="default" size="100%">Bioenergy Research </style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">Pathway</style></keyword><keyword><style  face="normal" font="default" size="100%">Penicillium</style></keyword><keyword><style  face="normal" font="default" size="100%">regulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Secretion</style></keyword><keyword><style  face="normal" font="default" size="100%">Transport</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">16</style></volume><pages><style face="normal" font="default" size="100%">61-73</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	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.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	3.6&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sankar, Meena</style></author><author><style face="normal" font="default" size="100%">Mathew, Reshma M.</style></author><author><style face="normal" font="default" size="100%">Puthiyamadam, Anoop</style></author><author><style face="normal" font="default" size="100%">Sreeja-Raju, Athiraraj</style></author><author><style face="normal" font="default" size="100%">Christopher, Meera</style></author><author><style face="normal" font="default" size="100%">Gokhale, Digambar Vitthal</style></author><author><style face="normal" font="default" size="100%">Sukumaran, Rajeev K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Comparison of the solid-state and submerged fermentation derived secretomes of hyper-cellulolytic Penicillium janthinellum NCIM 1366 reveals the changes responsible for differences in hydrolytic performance</style></title><secondary-title><style face="normal" font="default" size="100%">Bioresource Technology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Cellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">Solid -state fermentation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">371</style></volume><pages><style face="normal" font="default" size="100%">128602</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	better hydrolytic performance along with a higher initial rate of reaction. Secretome analyses of the SSF and SmF enzymes using LC/MS-MS, indicated that while the type of proteins secreted were similar in both modes, the abundance of specific beta glucosidases, lytic polysaccharide monooxygenases and hemicellulolytic enzymes were very high in SSF resulting in efficient initiation, low accumulation of cellobiose and high initial reaction rates. Key enzymes that catalyse lignocellulose breakdown under SSF and SmF are therefore different and the fungus may be speculated to have regulation mechanisms that aid differential expression under different culti&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	11.889&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Christopher, Meera</style></author><author><style face="normal" font="default" size="100%">Sreeja-Raju, Athiraraj</style></author><author><style face="normal" font="default" size="100%">Abraham, Amith</style></author><author><style face="normal" font="default" size="100%">Gokhale, Digambar Vitthal</style></author><author><style face="normal" font="default" size="100%">Pandey, Ashok</style></author><author><style face="normal" font="default" size="100%">Sukumaran, Rajeev K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Early cellular events and potential regulators of cellulase induction in Penicillium janthinellum NCIM 1366</style></title><secondary-title><style face="normal" font="default" size="100%">Scientific Reports</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">13</style></volume><pages><style face="normal" font="default" size="100%">5057</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Cellulase production by fungi is tightly regulated in response to environmental cues, and understanding this mechanism is a key pre-requisite in the efforts to improve cellulase secretion. Based on UniProt descriptions of secreted Carbohydrate Active enZymes (CAZymes), 13 proteins of the cellulase hyper-producer Penicillium janthinellum NCIM 1366 (PJ-1366) were annotated as cellulases- 4 cellobiohydrolases (CBH), 7 endoglucanases (EG) and 2 beta glucosidases (BGL). Cellulase, xylanase, BGL and peroxidase activities were higher for cultures grown on a combination of cellulose and wheat bran, while EG was stimulated by disaccharides. Docking studies indicated that the most abundant BGL- Bgl2- has different binding sites for the substrate cellobiose and the product glucose, which helps to alleviate feedback inhibition, probably accounting for the low level of glucose tolerance exhibited. Out of the 758 transcription factors (TFs) differentially expressed on cellulose induction, 13 TFs were identified whose binding site frequencies on the promoter regions of the cellulases positively correlated with their abundance in the secretome. Further, correlation analysis of the transcriptional response of these regulators and TF-binding sites on their promoters indicated that cellulase expression is possibly preceded by up-regulation of 12 TFs and down-regulation of 16 TFs, which cumulatively regulate transcription, translation, nutrient metabolism and stress response.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
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	4.6&lt;/p&gt;
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