@article {46616, title = {Penicillium janthinellum NCIM1366 shows improved biomass hydrolysis and a larger number of CAZymes with higher induction levels over Trichoderma reesei RUT-C30}, journal = {Biotechnology for Biofuels}, volume = {13}, year = {2020}, month = {DEC }, pages = {196}, type = {Article}, abstract = {

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.

}, keywords = {Bioethanol, CAZymes, Cellulase, Penicillium janthinellum, Secretome, Trichoderma reesei}, doi = {10.1186/s13068-020-01830-9}, author = {Sreeja-Raju, Athiraraj and Christopher, Meera and Kooloth-Valappil, Prajeesh and Kuni-Parambil, Rajasree and Gokhale, Digambar Vittal and Sankar, Meena and Abraham, Amith and Pandey, Ashok and Sukumaran, Rajeev K.} } @article {48093, title = {Assembly, annotation, and comparative whole genome sequence of fusarium verticillioides isolated from stored maize grains}, volume = {11}, year = {2022}, month = {JUL}, pages = {810}, type = {Article}, abstract = {

Fusarium verticillioides is a plant pathogenic fungus affecting a wide range of crops worldwide due to its toxigenic properties. F. verticillioides BIONCL4 strain was isolated from stored maize grain samples in India, and produces high amount of fumonisin B1 (FB1). We report a comparative genomic analysis of F. verticillioides, covering the basic genome information, secretome, and proteins involved in host-pathogen interactions and mycotoxin biosynthesis. Whole-genome sequencing (WGS) was performed using the Illumina platform with an assembly size of 42.91 Mb, GC content of 48.24\%, and 98.50\% coverage with the reference genome (GCA000149555). It encodes 15,053 proteins, including 2058 secretory proteins, 676 classical secretory proteins, and 569 virulence and pathogenicity-related proteins. There were also 1447 genes linked to carbohydrate active enzymes (CaZymes) and 167 genes related to mycotoxin production. Furthermore, F. verticillioides genome comparison revealed information about the species{\textquoteright} evolutionary history. The overall study helps in disease prevention and management of mycotoxins to ensure food safety.

}, keywords = {comparative genomics, Fusarium verticillioides, mycotoxin biosynthesis, plant-pathogen interaction, Secretome, whole-genome sequencing}, doi = {10.3390/pathogens11070810}, author = {Navale, Vishwambar D. and Sawant, Amol M. and Gowda, Varun U. and Vamkudoth, Koteswara Rao} } @article {48220, title = {Lignocellulose degradation by Penicillium janthinellum enzymes is influenced by its variable secretome and a unique set of feedstock characteristics}, journal = {Bioresource Technology}, volume = {365}, year = {2022}, month = {DEC}, pages = {128129}, type = {Article}, abstract = {

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.

}, keywords = {Biofuel, CAZyme, Cellulase, Penicillium, Secretome}, issn = {0960-8524}, doi = {10.1016/j.biortech.2022.128129}, author = {Christopher, Meera and Sreeja-Raju, Athiraraj and Sankar, Meena and Gokhale, Digambar Vitthal and Pandey, Ashok and Sukumaran, Rajeev K.} }