<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kumar, Umesh</style></author><author><style face="normal" font="default" size="100%">Shete, Ashvini</style></author><author><style face="normal" font="default" size="100%">Harle, Arti S.</style></author><author><style face="normal" font="default" size="100%">Kasyutich, Oksana</style></author><author><style face="normal" font="default" size="100%">Schwarzacher, W.</style></author><author><style face="normal" font="default" size="100%">Pundle, Archana</style></author><author><style face="normal" font="default" size="100%">Poddar, Pankaj</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Extracellular bacterial synthesis of protein-functionalized ferromagnetic Co3O4 nanocrystals and imaging of self-organization of bacterial cells under stress after exposure to metal ions</style></title><secondary-title><style face="normal" font="default" size="100%">Chemistry of Materials</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</style></number><publisher><style face="normal" font="default" size="100%">AMER CHEMICAL SOC</style></publisher><pub-location><style face="normal" font="default" size="100%">1155 16TH ST, NW, WASHINGTON, DC 20036 USA</style></pub-location><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">1484-1491</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Co3O4, which crystallizes in the spinet phase at temperatures much higher than ambient temperatures, orders antiferromagnetically below its Neel temperature (similar to 40 K). However, in nanosize, it shows ferromagnetic ordering due to surface canting, disorder, imperfect oxygen atom coordination, etc. Here, for the first time, we report the synthesis of single-crystalline, ferromagnetic Co3O4 nanoparticles functionalized with proteins (size 5-7 nm) using cobalt acetate as precursor at room temperature in aqueous medium by a metal-tolerant marine bacterium isolated from the coast of the Arabian Sea. Energetically unfavorable change in the oxidation state of Co atoms from (+2 to +3) during synthesis by the bacterial strain was evidenced by X-ray photoelectron spectroscopy. The effect on the morphology of bacterial cells after exposure to the cobalt acetate was imaged by scanning electron microscopy showing cooperative, self-organized. structured colony formation, possibly due to the interbacterial communication under external stress.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">9.407</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chavan, Sambhaji</style></author><author><style face="normal" font="default" size="100%">Shete, Ashvini</style></author><author><style face="normal" font="default" size="100%">Mirza, Yasmin</style></author><author><style face="normal" font="default" size="100%">Dharne, Mahesh S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Investigation of cold-active and mesophilic cellulases: opportunities awaited</style></title><secondary-title><style face="normal" font="default" size="100%">Biomass Conversion and Biorefinery</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">cellulases</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycosyl hydrolase</style></keyword><keyword><style  face="normal" font="default" size="100%">Lignocellulosic biomass</style></keyword><keyword><style  face="normal" font="default" size="100%">Metagenomics</style></keyword><keyword><style  face="normal" font="default" size="100%">simultaneous saccharification and fermentation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">13</style></volume><pages><style face="normal" font="default" size="100%">8829-8852</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	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.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><work-type><style face="normal" font="default" size="100%">Review</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
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	4&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chavan, Sambhaji</style></author><author><style face="normal" font="default" size="100%">Shete, Ashvini</style></author><author><style face="normal" font="default" size="100%">Dharne, Mahesh S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Strain improvement for cellulolytic enzymes for effective saccharification of lignocellulosic biomass by mutant of Penicillium funiculosum NCIM 1228</style></title><secondary-title><style face="normal" font="default" size="100%">Systems Microbiology and Biomanufacturing</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2024</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">716–730</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	&lt;span style=&quot;font-family: Merriweather, serif; font-size: 18px;&quot;&gt;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.&amp;nbsp;&lt;/span&gt;&lt;i style=&quot;box-sizing: inherit; font-family: Merriweather, serif; font-size: 18px;&quot;&gt;Penicillium funiculosum&lt;/i&gt;&lt;span style=&quot;font-family: Merriweather, serif; font-size: 18px;&quot;&gt;&amp;nbsp;NCIM 1228 (&lt;/span&gt;&lt;i style=&quot;box-sizing: inherit; font-family: Merriweather, serif; font-size: 18px;&quot;&gt;P. funiculosum&lt;/i&gt;&lt;span style=&quot;font-family: Merriweather, serif; font-size: 18px;&quot;&gt;&amp;nbsp;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&amp;nbsp;g/L at the 40&amp;nbsp;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.&lt;/span&gt;&lt;/p&gt;
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	Foreign&lt;/p&gt;
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	NA&lt;/p&gt;
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