As the need for non-renewable sources such as fossil fuels has increased during the last few decades, the search for sustainable and renewable alternative sources has gained growing interest. Enzymatic hydrolysis in bioethanol production presents an important step, where sugars that are fermented are obtained in the final fermentation process. In the process of enzymatic hydrolysis, more and more new effective enzymes are being researched to ensure a more cost-effective process. There are many different enzyme strategies implemented in hydrolysis protocols, where different lignocellulosic biomass, such as wood feedstocks, different agricultural wastes, and marine algae are being used as substrates for an efficient bioethanol production. This review investigates the very recent enzymatic hydrolysis pathways in bioethanol production from lignocellulosic biomass.

The development of solid acid catalysts, especially based on metal oxides and different magnetic nanoparticles, gained much awareness recently as a result of the development of different nano-based materials. Solid acid catalysts based on metal oxides are promising for the (trans)esterification reactions of different oils and waste materials for biodiesel production. This review gives a brief overview of recent developments in various solid acid catalysts based on different metal oxides, such as zirconia, zinc, titanium, iron, tungsten, and magnetic materials, where the catalysts are optimized for various reaction parameters, such as the amount of catalyst, molar ratio of oil to alcohol, reaction time, and temperature. Furthermore, yields and conversions for biodiesel production are compared. Such metal-oxide-based solid acid catalysts provide more sustainable, green, and easy-separation synthesis routes with high catalytic activity and reusability than traditionally used catalysts.

A wide range of applications using functionalized magnetic nanoparticles (MNPs) in biomedical applications, such as in biomedicine as well as in biotechnology, have been extensively expanding over the last years. Their potential is tremendous in delivery and targeting systems due to their advantages in biosubstance binding. By applying magnetic materials-based biomaterials to different organic polymers, highly advanced multifunctional bio-composites with high specificity, efficiency, and optimal bioavailability are designed and implemented in various bio-applications. In modern drug delivery, the importance of a successful therapy depends on the proper targeting of loaded bioactive components to specific sites in the body. MNPs are nanocarrier-based systems that are magnetically guided to specific regions using an external magnetic field. Therefore, MNPs are an excellent tool for different biomedical applications, in the form of imaging agents, sensors, drug delivery targets/vehicles, and diagnostic tools in managing disease therapy. A great contribution was made to improve engineering skills in surgical diagnosis, therapy, and treatment, while the advantages and applicability of MNPs have opened up a large scope of studies. This review highlights MNPs and their synthesis strategies, followed by surface functionalization techniques, which makes them promising magnetic biomaterials in biomedicine, with special emphasis on drug delivery. Mechanism of the delivery system with key factors affecting the drug delivery efficiency using MNPs are discussed, considering their toxicity and limitations as well.

Due to the growing awareness of Punica granatum fruit’s health-promoting properties, the pomegranate is increasingly used for food purposes. This results in the formation of biological waste products such as peels. A biowaste circular bioeconomy strategy holds great prospective for a sustainable economy. Therefore, a sustainable and environmentally friendly way of disposing of waste (e.g., use of biowaste to obtain high-value components (e.g., punicalagins, enzymes)) is crucial for the protection of the environment and human health. In the presented study, the content of total phenols and proanthocyanidins in ten samples of Punica granatum fruit (juice, aqueous (H₂O) and ethanolic (EtOH) extracts of peels and seeds) was determined. Peel extracts were found to be the richest in the content of secondary metabolites and showed extremely high antioxidant potential (approximately 90% inhibition: DPPH radical scavenging activity). To the best of our knowledge, this is the first comparative study to determine the enzymatic activity of α-amylase, lipase, peroxidase, protease, and transglutaminase in different P. granatum samples. Furthermore, the antibacterial efficacy of all P. granatum samples was qualitatively determined against three strains of Gram-negative (Escherichia coli, Pseudomonas aeruginosa, and Pseudomonas fluorescens) and three strains of Gram-positive (Bacillus cereus, Staphylococcus aureus, and Streptococcus pyogenes) bacteria, susceptible to gaining antibiotic resistance. Moreover, the most promising peel extracts were quantified for antibacterial efficacy against tested bacteria at five different concentrations. All samples slowed down and inhibited the growth of all tested bacteria. MIC₉₀ values (2.7 or 0.3 mg/mL) were determined in 18 out of 24 experiments (four samples, six bacteria tested). There is no research in the reviewed literature that is current with such detailed and comprehensive determination of P. granatum peel extracts antibacterial activity. The results of the research showed great potential for the use of P. granatum in the field of antibacterial activity in biomedicine applications and in the cosmetic, food, and pharmaceutical industries.

Stabilization and reusability of enzyme transglutaminase (TGM) are important goals for the enzymatic process since immobilizing TGM plays an important role in different technologies and industries. TGM can be used in many applications. In the food industry, it plays a role as a protein-modifying enzyme, while, in biotechnology and pharmaceutical applications, it is used in mediated bioconjugation due to its extraordinary crosslinking ability. TGMs (EC 2.3.2.13) are enzymes that catalyze the formation of a covalent bond between a free amino group of protein-bound or peptide-bound lysine, which acts as an acyl acceptor, and the γ-carboxamide group of protein-bound or peptide-bound glutamine, which acts as an acyl donor. This results in the modification of proteins through either intramolecular or intermolecular crosslinking, which improves the use of the respective proteins significantly.