<?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%">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;
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