@article {46806, title = {Efficacy of octahedral molecular sieves for green and sustainable catalytic reactions}, journal = {Molecular Catalysis}, volume = {490}, year = {2020}, month = {JUL}, pages = {110966}, type = {Review}, abstract = {

Sustainability and Green Chemistry has emerged as catchphrase in modern era and researchers worldwide have embraced it as new paradigm of development. In this context identifying potential materials able to curb multiple grave issues thus contributing towards sustainability is vital. Catalytic materials are quite potent for addressing current social, economic and environmental problems like harnessing alternative energy source, pollution prevention/remediation and manufacturing of commodity chemicals. Thus, the present review accentuates the efficacy of porous octahedral molecular sieves (OMS) as catalyst for such environmentally important reactions. It discusses about structural importance of OMS and their applications for green and sustainable catalytic reactions. Finally, the limitations are highlighted and future perspectives are presented which will ameliorate its catalytic utilization in energy and environmental domains.

}, keywords = {catalytic transformations, Lignocellulosic biomass, octahedral molecular sieves, platform chemicals, renewable feedstock}, issn = {2468-8231}, doi = {10.1016/j.mcat.2020.110966}, author = {Lucas, Nishita and Gurrala, Lakshmiprasad and Halligudi, S. B.} } @article {49131, title = {Investigation of cold-active and mesophilic cellulases: opportunities awaited}, journal = {Biomass Conversion and Biorefinery}, volume = {13}, year = {2023}, month = {JUL}, pages = {8829-8852}, type = {Review}, abstract = {

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.

}, keywords = {cellulases, Glycosyl hydrolase, Lignocellulosic biomass, Metagenomics, simultaneous saccharification and fermentation}, issn = {2190-6815}, doi = {10.1007/s13399-021-02047-y}, author = {Chavan, Sambhaji and Shete, Ashvini and Mirza, Yasmin and Dharne, Mahesh S.} } @article {48960, title = {Bioprocess optimization of penicillium funiculosum NCIM 1228 for improved production and hydrolytic efficiency of cellulases on sugarcane bagasse}, journal = {Sugar Tech}, volume = {26}, year = {2024}, month = {FEB}, pages = {215-233}, type = {Journal Article}, abstract = {

The cellulase enzyme is currently the world{\textquoteright}s third largest commercial enzyme. Because of its requirement in various industries like textiles, food, waste management, pharmaceuticals, agriculture, pulp paper, biofuels, and others, its demand curve has increased sharply. The response surface methodology (RSM) approach was employed to optimize media components and process parameters in the current investigation, which successfully increased the cellulase production from Penicillium funiculosum NCIM 1228. Statistical optimization for the hyperproduction of cellulases was conducted using RSM. The Plackett-Burman design (PBD) approach was used to investigate the critical factors of the cellulase production medium. Subsequently, the Box-Behnken design (BBD) method was used to statistically estimate optimum values and conditions that substantially impacted cellulase production. The estimated optimal combinations of parameters for cellulase production were urea (0.2\%), CaCl2 (0.2\%), MgSO4 (0.05\%), peptone (1.5\%), microcrystalline cellulose (5.0\%), wheat bran (2.5\%), corn steep liquor (CSL) (2.5\%), KH2PO4 (0.15\%), inoculum (10.65\%), agitation (157 rpm), pH (5.88), and temperature (29.84 C-degrees). Conclusively, experimental validation under optimal conditions detected an increased production of 3.82- and 3.61-fold in filter paper assay (FPase) and beta-glucosidase, respectively. Additionally, 1.66- and 1.57-fold enhancement in FPase and beta-glucosidase specific activity was observed where an xylanase activity was enhanced by 3.29-fold. Furthermore, the enzyme showed 51.30 per cent hydrolysis efficiency on sugarcane bagasse lignocellulosic biomass (LCB), at a dose of 7 FPase units per g of cellulose. P. funiculosum NCIM 1228 offers the benefit of producing cellulase with an entire cellulolytic system of enzymes that can be synthesized extracellularly, thus acting as a promising biocatalyst for biofuel industries.

}, keywords = {Cellulase, Lignocellulosic biomass, Penicillium funiculosum, Response surface methodology, Submerged fermentation, Xylanase}, issn = {0972-1525}, doi = {10.1007/s12355-023-01324-6}, author = {Chavan, Sambhaji B. and Shete, Ashvini M. and Dharne, Mahesh S.} }