<?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%">Jayamurthy, Himani</style></author><author><style face="normal" font="default" size="100%">Sajna, Kuttavan Valappil</style></author><author><style face="normal" font="default" size="100%">Dastager, Syed Gulam</style></author><author><style face="normal" font="default" size="100%">Pandey, Ashok</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Anti-fungal potentials of extracellular metabolites of western ghats isolated streptomyces sp NII 1006 against moulds and yeasts</style></title><secondary-title><style face="normal" font="default" size="100%">Indian Journal of Experimental Biology </style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Anti-fungal activity</style></keyword><keyword><style  face="normal" font="default" size="100%">Biocontrol</style></keyword><keyword><style  face="normal" font="default" size="100%">Extracellular anti-fungal metabolites</style></keyword><keyword><style  face="normal" font="default" size="100%">Streptomyces</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">11</style></number><publisher><style face="normal" font="default" size="100%">NATL INST SCIENCE COMMUNICATION-NISCAIR</style></publisher><pub-location><style face="normal" font="default" size="100%">DR K S KRISHNAN MARG, PUSA CAMPUS, NEW DELHI 110 012, INDIA</style></pub-location><volume><style face="normal" font="default" size="100%">52</style></volume><pages><style face="normal" font="default" size="100%">1138-1146</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Realization of hazardious effects of chemical fungicides has led to an interest in the usage of biocontrol agents. The present study, therefore, evaluates the biocontrol efficacy of Western Ghats (India) soil bacterial isolates. A potential strain NII 1006 was evaluated for its antagonistic property against a diverse range of moulds and yeasts. The strain was characterized morphologically, biochemically and molecularly, which revealed the isolate belonged to Streptomyces genus. Organic solvent extracts of NII 1006 culture filtrates inhibited the growth of the test pathogens indicating that growth suppression was due to extracellular anti-fungal metabolites present in the culture filtrates. The strain produced extracellular chitinase enzyme in addition to some stable partially purified anti-fungal compounds. Morphological changes such as hyphae degradation into debris and abnormal shapes were observed in test fungi and yeast grown on potato dextrose broth that contained the NII 1006 culture filtrate. The cell free supernatant has a tolerance to wide range of pH, temperature and enzymes such as lipase and protease. The biocontrol potential of NII 1006 strain may be correlated significantly with their ability to produce antibiotics as well as extracellular hydrolytic enzymes particularly chitinolytic enzyme.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">11</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Indian</style></custom3><custom4><style face="normal" font="default" size="100%">1.165</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%">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%">Kooloth-Valappil, Prajeesh</style></author><author><style face="normal" font="default" size="100%">Kuni-Parambil, Rajasree</style></author><author><style face="normal" font="default" size="100%">Gokhale, Digambar Vittal</style></author><author><style face="normal" font="default" size="100%">Sankar, Meena</style></author><author><style face="normal" font="default" size="100%">Abraham, Amith</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%">Penicillium janthinellum NCIM1366 shows improved biomass hydrolysis and a larger number of CAZymes with higher induction levels over Trichoderma reesei RUT-C30</style></title><secondary-title><style face="normal" font="default" size="100%">Biotechnology for Biofuels</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bioethanol</style></keyword><keyword><style  face="normal" font="default" size="100%">CAZymes</style></keyword><keyword><style  face="normal" font="default" size="100%">Cellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">Penicillium janthinellum</style></keyword><keyword><style  face="normal" font="default" size="100%">Secretome</style></keyword><keyword><style  face="normal" font="default" size="100%">Trichoderma reesei</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</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%">13</style></volume><pages><style face="normal" font="default" size="100%">196</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Background Major cost of bioethanol is attributed to enzymes employed in biomass hydrolysis. Biomass hydrolyzing enzymes are predominantly produced from the hyper-cellulolytic mutant filamentous fungus Trichoderma reesei RUT-C30. Several decades of research have failed to provide an industrial grade organism other than T. reesei, capable of producing higher titers of an effective synergistic biomass hydrolyzing enzyme cocktail. Penicillium janthinellum NCIM1366 was reported as a cellulase hyper producer and a potential alternative to T. reesei, but a comparison of their hydrolytic performance was seldom attempted. Results Hydrolysis of acid or alkali-pretreated rice straw using cellulase enzyme preparations from P. janthinellum and T. reesei indicated 37 and 43% higher glucose release, respectively, with P. janthinellum enzymes. A comparison of these fungi with respect to their secreted enzymes indicated that the crude enzyme preparation from P. janthinellum showed 28% higher overall cellulase activity. It also had an exceptional tenfold higher beta-glucosidase activity compared to that of T. reesei, leading to a lower cellobiose accumulation and thus alleviating the feedback inhibition. P. janthinellum secreted more number of proteins to the extracellular medium whose total concentration was 1.8-fold higher than T. reesei. Secretome analyses of the two fungi revealed higher number of CAZymes and a higher relative abundance of cellulases upon cellulose induction in the fungus. Conclusions The results revealed the ability of P. janthinellum for efficient biomass degradation through hyper cellulase production, and it outperformed the established industrial cellulase producer T. reesei in the hydrolysis experiments. A higher level of induction, larger number of secreted CAZymes and a high relative proportion of BGL to cellulases indicate the possible reasons for its performance advantage in biomass hydrolysis.&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;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;4.815&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%">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;
</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;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	4.6&lt;/p&gt;
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