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

TitleCellulase hyper-producing fungus penicillium janthinellum NCIM 1366 elaborates a wider array of proteins involved in transport and secretion, potentially enabling a diverse substrate range
Publication TypeJournal Article
Year of Publication2023
AuthorsChristopher, M, Sreeja-Raju, A, Kooloth-Valappil, P, Gokhale, DVitthal, Sukumaran, RK
JournalBioenergy Research
Volume16
Pagination61-73
Date PublishedMAR
Type of ArticleArticle
ISSN1939-1234
KeywordsCellulase, Pathway, Penicillium, regulation, Secretion, Transport
Abstract

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.

DOI10.1007/s12155-022-10407-3
Type of Journal (Indian or Foreign)

Foreign

Impact Factor (IF)

3.6

Divison category: 
National Collection of Industrial Micr-organisms (NCIM)
Database: 
Web of Science (WoS)

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