Green synthesis of silver (Ag) and gold (Au) nanoparticles (NPs) has acquired huge popularity owing to their potential applications in various fields. A large number of research articles exist in the literature describing the green synthesis of Ag and Au NPs for biomedical applications. However, these findings are scattered, making it time-consuming for researchers to locate promising advancements in Ag and Au NPs synthesis and their unexplored biomedical applications. Unlike other review articles, this systematic study not only highlights recent advancements in the green synthesis of Ag and Au NPs but also explores their potential unexplored biomedical applications. The article discusses the various synthesis approaches for the green synthesis of Ag and Au NPs highlighting the emerging developments and novel strategies. Then, the article reviews the important biomedical applications of green synthesized Ag and Au NPs by critically evaluating the expected advantages. To expose future research direction in the field, the article describes the unexplored biomedical applications of the NPs. Finally, the articles discuss the challenges and limitations in the green synthesis of Ag and Au NPs and their biomedical applications. This article will serve as a valuable reference for researchers, working on green synthesis of Ag and Au NPs for biomedical applications.

To increase its operational stability and ongoing reusability, B. subtilis pectinase was immobilized on iron oxide nanocarrier. Through co-precipitation, magnetic iron oxide nanoparticles were synthesized. Scanning electron microscopy (SEM) and energy dispersive electron microscopy (EDEX) were used to analyze the nanoparticles. Pectinase was immobilized using glutaraldehyde as a crosslinking agent on iron oxide nanocarrier. In comparison to free pectinase, immobilized pectinase demonstrated higher enzymatic activity at a variety of temperatures and pH levels. Immobilization also boosted pectinase’s catalytic stability. After 120 h of pre-incubation at 50 °C, immobilized pectinase maintained more than 90% of its initial activity due to the iron oxide nanocarrier, which improved the thermal stability of pectinase at various temperatures. Following 15 repetitions of enzymatic reactions, immobilized pectinase still exhibited 90% of its initial activity. According to the results, pectinase’s catalytic capabilities were enhanced by its immobilization on iron oxide nanocarrier, making it economically suitable for industrial use.

Co-culture of Bacillus coagulans and Candida utilis was firstly investigated in the efficient treatment of Lactobacillus fermentation wastewater (LFW) containing total organic carbon (TOC) of 22.0 g/L and total nitrogen (TN) of 2.4 g/L. The utilization of lactic acid by C. utilis was responsible for the relief of feedback inhibition to promote the growth of B. coagulans. The removal ratio of TOC by B. coagulans and C. utilis was only 9.1% and 22.7%, respectively, which was improved to 49.0% by co-culture. The removal ratio of TN by B. coagulans and C. utilis was merely 6.3% and 12.5%, respectively, which was also promoted to 44.6% by co-culture. Both the high growth of B. coagulans and the efficient removal of TOC and TN from LFW was achieved with the co-culture, which is not previously reported and very important in the production of probiotics with the resource utilization of LFW.

Cholesterol (CHOL) is one of the risk factors causing the blockage of the arterial wall, atherosclerosis, coronary heart disease, and other serious cardiovascular diseases. Here, a promising bacterial strain for biodegrading CHOL was successfully isolated from the gut of healthy individuals and identified as Enterococcus faecium YY01 with an analysis of the 16S rDNA sequence. An initial CHOL of 1.0 g/L was reduced to 0.5 g/L in 5 days, and glucose and beef extract were found to be optimal carbon and nitrogen sources for the rapid growth of YY01, respectively. To gain further insight into the mechanisms underlying CHOL biodegradation, the draft genome of YY01 was sequenced using Illumina HiSeq. Choloylglycine hydrolase, acyltransferase, and alkyl sulfatase was encoded by gene0586, gene1890, and gene2442, which play crucial roles in converting 3α, 7α, 12α-trihydroxy-5β-choranic acid to choline-CoA and then choline-CoA to bile acid. Notably, choloylglycine hydrolase was closely related to the biosynthesis of both primary and secondary bile acid. The findings of this study provide valuable insights into the metabolism pathway of CHOL biodegradation by YY01 and offer a potential avenue for the development of bacterioactive drugs against hypercholesterolemia.