03006nas a2200301 4500008004100000245016400041210006900205260000900274300000800283490000700291520195400298653001502252653001202267653001402279653002902293653001402322653002302336100002702359700002302386700003102409700002802440700003002468700001802498700001902516700001802535700002602553856012502579 2020 eng d00aPenicillium janthinellum NCIM1366 shows improved biomass hydrolysis and a larger number of CAZymes with higher induction levels over Trichoderma reesei RUT-C300 aPenicillium janthinellum NCIM1366 shows improved biomass hydroly cDEC  a1960 v133 a

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.

10aBioethanol10aCAZymes10aCellulase10aPenicillium janthinellum10aSecretome10aTrichoderma reesei1 aSreeja-Raju, Athiraraj1 aChristopher, Meera1 aKooloth-Valappil, Prajeesh1 aKuni-Parambil, Rajasree1 aGokhale, Digambar, Vittal1 aSankar, Meena1 aAbraham, Amith1 aPandey, Ashok1 aSukumaran, Rajeev, K. uhttps://library.ncl.res.in/content/penicillium-janthinellum-ncim1366-shows-improved-biomass-hydrolysis-and-larger-number02073nas 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

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.

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-variable01622nas a2200241 4500008004100000022001400041245021100055210006900266260000800335300001100343490000800354520067500362653001401037653003001051100001801081700002301099700002401122700002701146700002301173700003101196700002601227856012701253 2023 eng d a0960-852400aComparison of the solid-state and submerged fermentation derived secretomes of hyper-cellulolytic Penicillium janthinellum NCIM 1366 reveals the changes responsible for differences in hydrolytic performance0 aComparison of the solidstate and submerged fermentation derived  cMAR a1286020 v3713 a

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

10aCellulase10aSolid -state fermentation1 aSankar, Meena1 aMathew, Reshma, M.1 aPuthiyamadam, Anoop1 aSreeja-Raju, Athiraraj1 aChristopher, Meera1 aGokhale, Digambar, Vitthal1 aSukumaran, Rajeev, K. uhttps://library.ncl.res.in/content/comparison-solid-state-and-submerged-fermentation-derived-secretomes-hyper-cellulolytic