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Molecular interactions are crucial between the enzyme molecules and the surrounding solution in an enzymatic catalysis. Although aqueous solutions used as conventional enzymatic reaction media, non-aqueous enzymology emerges as a major area of biotechnology research and development. Ionic liquids, as new generation of promising alternatives to traditional organic solvents, possess potential industrial enzymatic applications. Enzymes in ionic liquids present enhanced activity, stability, and selectivity. In addition, the potential of ionic liquids in bio-catalysis is raised by high ability of dissolving a wide variety of substrates and their extensively tunable solvent properties through appropriate modification of the cations and anions. However, despite the bio-friendly nature of ionic liquids for enzymatic reactions, their growing interests increase concerns associated with toxicity and environmental pollution of such compounds. This mini-review presents a brief highlight of the contemporary knowledge of enzymes activity and stability in ionic liquids and the environmental influences regarding the potential risks related to the growing applications of these green solvents. HIGHLIGHTS •Conventional organic solvents can be replaced by ionic liquids as green solvents. •Ionic liquids are used as additives, catalysts, or reaction media in industries. •Advantages and disadvantages of ionic liquids are discussed. •Potential environmental hazards linked to application of ionic liquids are highlighted. •The environmental fate needs to be considered in designing safer ionic liquids.

Despite the progress in treatment of infectious diseases, ability of microorganisms to develop the resistance to routine antibiotics has still remained as a big global challenge in clinics. This subject matter keeps the infections top in the list of life threatening diseases especially in those individuals suffering from nosocomial infections. The importance of this global health challenge urges researchers to find an alternative solution with more efficacies to treat infections. There are some alternative approaches by which the global spread of resistant bacteria could be controlled. Through these ways, using bacteriophages instead of different generation of antibiotics brings many promises. According to results of different studies using bacteriophages in the management of infectious disease especially in nosocomial infections not only helps to reduce the spread of antibiotics resistance but also raises the hopes for the rescue of the suffering patients. Bacteriophages can open a new therapeutic window in the control and the treatment of the infectious disease with better efficacy. HIGHLIGHTS •Bacteriophage can be used as an antimicrobial agent for treatment of bacterial infection. •Bacterial resistance to routine antibiotics is a big challenge in the world. •Specificity toward bacteria is one of the important characteristic of phages.

Lipases are the biocatalysts with outstanding prospects in industry and medicine. They have proven to be useful in various hydrolytic and synthetic reactions. However, there are some limitations for impure lipases that may restrict their widely uses in industrial applications. Purification is sometimes vital for the characterization of the function, structure, and interactions of lipases. The lipase immobilization is also an efficient strategy for increasing the enzyme activity and stability, and getting a simpler recovery. Lipases are naturally produced together with many other proteins that they may occupy some surface of immobilization solid support and decrease the final activity. The coupling of immobilization and purification of lipase will overcome the mentioned problems and obtain the maximum purification yields. The present mini-review will discuss the use of the techniques that permit to join immobilization and purification of lipases in a single step, including control of the immobilization conditions by interfacial activation on hydrophobic supports, the development of specific supports with affinity for lipases, and the use of bio-affinity supports including immuno- and lectin affinity HIGHLIGHTS •Lipases are the biocatalysts with outstanding prospects in industry and medicine. •Simultaneous immobilization-purification may enhance lipase activity and stability. •Lipases have a mechanism of interfacial activation in the presence of hydrophobic interfaces. •The lipase immobilization on hydrophobic supports is a much-utilized strategy. •Bio-affinity is a promising approach to increase lipase final yield and activity.

Stereo-selectivity is an important feature in the development of the synthesis of biologically active organic compounds. In this process, (bio) catalysts exhibit substrate specificity that allows high levels of chemo- and regio-selectivity. Over the past decade, several peptides have been developed as effective bio-catalysts for a range of synthetically valuable reactions. In comparison with proteins owing a large number of amino acids and high molecular weights, peptide-catalysts possess only a few amino acid residues, which may adopt a secondary structure suitable for synthesis of desired chiral products. In addition, the flexible nature of peptides consents for tuning of reactivity and selectivity by replacing amino acid residues. These unique aspects provide attractive biocatalysts platform for asymmetric syntheses. Highlights • Asymmetric catalysis has an impressive progression in the manufacture of pharmaceuticals. • Enzymes and natural/synthetic peptides are attractive biocatalysts of the chiral reactions. • Peptides show unique features compared with other catalysts in asymmetric catalysis.

Various proteins and enzymes produced during algal photosynthesis can be used in economic development and environment management, such as in wastewater treatment, production of fine chemicals, and biodiesel production. This mini-review presents various enzymes isolated from algae and suggests that algae, given their unique properties, could be explored for large-scale production of enzymes as future biocatalyst factories. Highlights • Various proteins and enzymes are produced during algal photosynthesis. • Algae use phosphoglycolate phosphatase and glycolate oxidase as metabolizing enzymes. • Algae possess the ability to produce commercial enzymes. • Out of the 10,000 algae species, only a few are cultivated on an industrial scale. • Algal wastes can be manipulated and recycled for production of various enzymes.