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Microalgae is a renewable bioresource with the potential to replace the conventional fossil-based industrial production of organic chemicals and pharmaceuticals. Moreover, the microalgal biomass contains carotenoids, vitamins, and other biomolecules that are widely used as food supplements. However, the microalgal biomass production, their composition variations, energy-intensive harvesting methods, optimized bio-refinery routes, and lack of techno-economic analysis are the major bottleneck for the life-sized commercialization of this nascent bio-industry. This review discusses the microalgae-derived key bioactive compounds and their applications in different sectors for human health. Furthermore, this review proposes advanced strategies to enhance the productivity of bioactive compounds and highlight the key challenges associated with a safety issue for use of microalgae biomass. It also provides a detailed global scenario and market demand of microalgal bioproducts. In conclusion, this review will provide the concept of microalgal biorefinery to produce bioactive compounds at industrial scale platform for their application in the nutraceutical and pharmaceutical sector considering their current and future market trends., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

Chemical programming of nine murine antibodies with catalytic aldolase activity was examined using compounds, equipped with diketone or pro-vinyl ketone linkers that inhibit integrin adhesion receptor functions. The results showed that most Abs were programmed using the diketone compounds in a manner similar to previously reported catalytic antibody 38C2. On the other hand, only those antibodies, which catalyzed the retro aldol reaction of the pro-vinyl ketone linkers efficiently, were programmed. Conjugated to integrin targeting compounds, at least three new antibodies, including 84G3, 85H6, and 90G8, exhibited high specific binding to human tumor cells expressing integrin alpha(v)beta(3.).

Irreversible chemical programming of monoclonal aldolase antibody (mAb) 38C2 has been accomplished with beta-lactam equipped mono- and bifunctional targeting modules, including a cyclic-RGD peptide linked to either the peptide (D-Lys(6))-LHRH or another cyclic RGD unit and a small-molecule integrin inhibitor SCS-873 conjugated to (D-Lys(6))LHRH. We also prepared monofunctional targeting modules containing either cyclic RGD or (D-Lys(6))-LHRH peptides. Binding of the chemically programmed antibodies to integrin receptors alpha(v)beta(3) and alpha(v)beta(5) and to the luteinizing hormone releasing hormone receptor were evaluated. The bifunctional and bivalent c-RGD/LHRH and SCS-783/LHRH, the monofunctional and tetravalent c-RGD/c-RGD, and the monofunctional bivalent c-RGD chemically programmed antibodies bound specifically to the isolated integrin receptor proteins as well as to integrins expressed on human melanoma M-21 cells. c-RGD/LHRH, SCS-783/LHRH, and LHRH chemically programmed antibodies bound specifically to the LHRH receptors expressed on human ovarian cancer cells. This approach provides an efficient, versatile, and economically viable route to high-valency therapeutic antibodies that target defined combinations of specific receptors. Additionally, this approach should be applicable to chemically programmed vaccines.