02594nas a2200241 4500008004100000022001400041245008200055210006900137260000800206300001400214490000700228520178900235653001502024653002302039653002802062653001702090653005102107100002102158700001902179700001802198700002302216856011302239 2023 eng d a2190-681500aInvestigation of cold-active and mesophilic cellulases: opportunities awaited0 aInvestigation of coldactive and mesophilic cellulases opportunit cJUL a8829-88520 v133 a

In the recent decade, the global demand and fuel prices have urged a need to track down an alternate resource. Second-generation (2G) biofuel from the lignocellulosic biomass (LCB) is trending as the fundamental alternative resource. Although LCB is the most abundantly available renewable resource, its commercialization into 2G biofuel technology is a major challenge. Efficient LCB hydrolysis requires a proper lignocellulolytic enzyme cocktail. In view to addressing this problem, several researchers are investigating for efficient enzymes to hydrolyze LCB. To date, there are very few commercial enzymes that aid in the breakdown of LCB, and these enzymes are traditionally isolated from culturable microbes. As only 1% of the microbes can be cultivated in the laboratory, the potentials of the uncultured remain under-explored. In the recent decade, advances in metagenomics using next-generation sequencing (NGS) technologies have revealed the vast diversity of hydrolytic enzymes and multiple domain proteins in the ecosystem. Aiming this, we focus our review on investigating efficient cold-active and mesophilic cellulases from the metagenome. India is an agro-based country with various climatic regions, ranging from warm and humid in the south to mild or moderate and cold or snowy in the Himalayan north; therefore, both cold-active and mesophilic cellulases are needed for LCB to ethanol. Along with downsizing, the conversion cost of LCB to fermentable sugars not only increases the enzymatic conversion but also increases the fermentation efficiency, which ultimately helps to commercialize the second-generation biofuel technology. Metagenomics is an evolving concept, and it has opened new horizons for the discovery of micro-organisms and new enzymes.

10acellulases10aGlycosyl hydrolase10aLignocellulosic biomass10aMetagenomics10asimultaneous saccharification and fermentation1 aChavan, Sambhaji1 aShete, Ashvini1 aMirza, Yasmin1 aDharne, Mahesh, S. uhttps://library.ncl.res.in/content/investigation-cold-active-and-mesophilic-cellulases-opportunities-awaited02809nas a2200157 4500008004100000245015300041210006900194260000800263300001400271490000600285520216700291100002102458700001902479700002302498856013002521 2024 eng d00aStrain improvement for cellulolytic enzymes for effective saccharification of lignocellulosic biomass by mutant of Penicillium funiculosum NCIM 12280 aStrain improvement for cellulolytic enzymes for effective saccha cFEB a716–7300 v43 a

Lignocellulosic biomass (LCB) generated from various agro-waste can be effectively used to manufacture a broad range of value-added products cost-effectively. However, the high cost of cellulases is still a major challenge in producing biofuels and biochemicals from LCB on an industrial scale. The enzyme output and activity of cellulase in the fermentation broth are closely linked in terms of enzyme manufacturing costs. Therefore, research on efficient fermentation processes of hyperactive fungi, and cost-effective recovery systems have been directed toward lowering enzyme costs and increasing overall enzyme production. Penicillium funiculosum NCIM 1228 (P. funiculosum NCIM 1228) is a feasible cellulase-producing strain that possesses all four enzymes required to efficiently hydrolyse LCB. The primary objective of this study was to employ random mutagenesis to increase enzymes titer, yield, and productivity. The potential mutant D4 (derived by Ethyl methanesulfonate (EMS) mutation) exhibited 6.47, 3.05, 3.03, and 3.19-fold higher activities of FPase, CMCase, β-glucosidase, and xylanase, respectively, compared to the parent strain. Mutant D4 demonstrated a promising protein titer of 17.96 g/L at the 40 L fermenter scale, with productivities of 479, 4249, and 6987 U/L/day for FPase, CMCase, and Xylanase, respectively, on the tenth day. Interestingly, the crude form of enzymes from the mutant demonstrated promising saccharification, releasing 3.54% of glucose and achieving a 54.03% of cellulose conversion efficiency without formulation. In comparison, a commercially formulated enzyme exhibited 53.07% efficiency against pre-treated sugarcane bagasse, indicating its promising potential for future applications.

1 aChavan, Sambhaji1 aShete, Ashvini1 aDharne, Mahesh, S. uhttps://library.ncl.res.in/content/strain-improvement-cellulolytic-enzymes-effective-saccharification-lignocellulosic-biomass