Search

The gradually increasing need for fossil fuels demands renewable biofuel substitutes. This has fascinated an increasing investigation to design innovative energy fuels that have comparable Physico-chemical and combustion characteristics with fossil-derived fuels. The efficient microbes for bioenergy synthesis desire the proficiency to consume a large quantity of carbon substrate, transfer various carbohydrates through efficient metabolic pathways, capability to withstand inhibitory components and other degradation compounds, and improve metabolic fluxes to synthesize target compounds. Metabolically engineered microbes could be an efficient methodology for synthesizing biofuel from cellulosic biomass by cautiously manipulating enzymes and metabolic pathways. This review offers a comprehensive perspective on the trends and advances in metabolic and genetic engineering technologies for advanced biofuel synthesis by applying various heterologous hosts. Probable technologies include enzyme engineering, heterologous expression of multiple genes, CRISPR-Cas technologies for genome editing, and cell surface display., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

Nanobiocatalysts are one of the most promising biomaterials produced by synergistically integrating advanced biotechnology and nanotechnology. These have a lot of potential to improve enzyme stability, function, efficiencyand engineering performance in bioprocessing. Functional nanostructures have been used to create nanobiocatalystsbecause of their specific physicochemical characteristics and supramolecular nature. This review covers a wide range of nanobiocatalysts including polymeric, metallic, silica and carbon nanocarriers as well as their recent developments in controlling enzyme activity. The enormous potential of nanobiocatalysts in bioprocessing in designing effective laboratory trials forapplications in various fields such as food, pharmaceuticals, biofuel, and bioremediation is also discussed extensively., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

Cellulase and beta-glucosidase production on steam pretreated spruce (SPS) with Trichoderma reesei Rut C30, Trichoderma atroviride TUB F-1505 and TUB F-1663 was investigated. The enzymes were compared in term of activity, temperature optima and hydrolytic capacity. The T. atroviride cellulases proved to have lower temperature optima for filter paper activity (FPA) assay (50 degrees C) and for hydrolysis of SPS (40 degrees C) than the Rut C30 enzymes (60 degrees C for FPA and 50 degrees C for hydrolysis). Due to high levels of extracellular beta-glucosidases, the T. atroviride enzyme supernatants hydrolyzed the washed SPS to glucose more efficiently than the enzymes produced by T. reesei. On the other hand, when the whole fermentation broths were used instead of the supernatants, thus the mycelium bound enzymes were also present, the hydrolytic capacity of T. reesei Rut C30 was enhanced by approximately 200%, while an improvement of only 15% was observed in case of the T. atroviride isolates.

Comparisons were made for phytase production using wheat bran (WB) and oilcakes as substrates in solid-state fermentation (SSF) by Mucor racemosus NRRL 1994. WB was also used as mixed substrate with oil cakes. Sesame oil cake (SOC) served as the best carbon source for phytase synthesis by the fungal strain as it gave the highest enzyme titres (30.6 U/gds). Groundnut oil cake (GOC) also produced a reasonably good quantity of enzyme (24.3 U/gds). Enzyme production on WB was surprisingly much less (almost 3.5 times less in comparison to SOC). Mixing WB with SOC (1:1 ratio) resulted in better phytase activity (32.2 U/gds). Optimization of various process parameters such as incubation time, initial moisture content and inoculum concentration was carried out using the single variable mode optimization technique. Under optimized conditions, the production of phytase reached 44.5 U/gds, which was almost 1.5-fold higher than the highest yield obtained with any individual substrate used in this study and was more than 4-fold higher than that obtained from WB.

Solid-state fermentation (SSF) was carried out using coconut oil cake (COC) as substrate for the production of alpha-amylase using a fungal culture of Aspergillus oryzae. Raw COC supported the growth of the culture, resulting in the production of 1372 U/gds alpha-amylase in 24 h. Process optimization using a single parameter mode showed enhanced enzyme titre, which was maximum (1827 U/gds) when SSF was carried out at 30 degrees C for 72 h using a substrate with 68% initial moisture. Supplementation with glucose and starch further enhanced enzyme titre, which was maximum (1911 U/gds) with 0.5% starch. However, maltose inhibited the enzyme production. Studies on the effect of addition of external organic and inorganic nitrogenous compounds further showed a positive impact on enzyme synthesis by the culture. Increase of 1.7-fold in the enzyme activity (3388 U/gds) was obtained when peptone at 1% concentration was added to the fermentation medium. The enzyme production was growth-related, the activity being the maximum when the fungal biomass was at its peak at 72 h. Use of COC as raw material for enzyme synthesis could be of great commercial significance. To the best of our knowledge this is the first report on alpha-amylase production using COC in SSF., (Copyright 2003 Elsevier Ltd.)

Aspergillus ficuum TUB F-1165 and Rhizopus oligosporus TUB F-1166 produced extra-cellular phytase during solid-state fermentation (SSF) using polystyrene as inert support. Maximal enzyme production (10.07 U/g dry substrate (U/gds) for A. ficuum and 4.52 U/gds for R. oligosporus) was observed when SSF was carried out with substrate pH 6.0 and moisture 58.3%, incubation temperature 30 degrees C, inoculum size of 1.3 x 10(7) spores/5 g substrate, for 72 h for A. ficuum and with substrate pH 7.0 and moisture 58.3%, incubation temperature 30 degrees C, inoculum size of 1 x 10(6) spores/5 g substrate for 96 h for R. oligosporus. Results indicated scope for production of phytase using polystyrene as inert support.

Phytases (myo-inositol hexakisphosphate phosphohydrolase, EC 3.1.3.8) catalyse the release of phosphate from phytate (mycoinositol hexakiphosphate). Several cereal grains, legumes and oilseeds, etc., store phosphorus as phytate. Environmental pollution due to the high-phosphate manure, resulting in the accumulation of P at various locations has raised serious concerns. Phytases appear of significant value in effectively controlling P pollution. They can be produced from a host of sources including plants, animals and micro-organisms. Microbial sources, however, are promising for their commercial exploitations. Strains of Aspergillus sp., chiefly A. ficuum and A. niger have most commonly been employed for industrial purposes. Phytases are considered as a monomeric protein, generally possessing a molecular weight between 40 and 100 kDa. They show broad substrate specificity and have generally pH and temperature optima around 4.5-6.0 and 45-60 degrees C. The crystal structure of phytase has been determined at 2.5 A resolution. Immobilization of phytase has been found to enhance its thermostability. This article reviews recent trends on the production, purification and properties of microbial phytases.