Biosensors play important roles in different applications such as medical diagnostics, environmental monitoring, food safety, and the study of biomolecular interactions. Highly sensitive, label-free and disposable biosensors are particularly desired for many clinical applications. In the past decade, film bulk acoustic resonators (FBARs) have been developed as biosensors because of their high resonant frequency and small base mass (hence greater sensitivity), lower cost, label-free capability and small size. This paper reviews the piezoelectric materials used for FBARs, the optimisation of device structures, and their applications as biosensors in a wide range of biological applications such as the detection of antigens, DNAs and small biomolecules. Their integration with microfluidic devices and high-throughput detection are also discussed.

No abstract

This paper reports a diode-end-pumped continuous-wave (CW) Nd:YAG laser operating at 946-nm by utilizing the 4F3/2-4I9/2 transition. We demonstrated that at an incident pump power of 27.7 W, an output power of 8.3-W could be achieved with a slope efficiency of 33.5%. To the best of our knowledge, this is the highest CW output power at 946 nm generated by LD end-pumped Nd:YAG lasers. By using intracavity frequency doubling with an LBO crystal, we further obtained a 473-nm blue laser with an output power of 1.2 W, achieving an optical-to-optical conversion efficiency of 7.1% at a pump power of 16.9 W. The short-term power instability of the blue laser was less than 1 %.

BsCsn46A, a GH46 family chitosanase from Bacillus subtilis, has great potential for industrial chitooligosaccharide production due to its high activity and stability. In this study, a special amino acid Pro121 was identified not fit in the helix structure, which was located in the opposite side of the active center in BsCsn46A, by the PoPMuSiC algorithm. Then, saturation mutagenesis was performed to explore the role of the site amino acid 121. Compared with the wild type, the specific activity of P121N, P121C, and P121V was increased by 1.69-, 1.97-, and 2.15-fold, respectively. In particular, the specific activity of P121N was increased without loss of thermostability, indicating that replacing the structural stiffness of proline in the helical structure could significantly improve the chitosanase activity. The K m values of P121N, P121C, and P121V decreased significantly, indicating that the affinity between the enzyme–substrate complex was enhanced. Through molecular docking, it was found that the increase of hydrogen bonds and van der Waals force between the enzyme–substrate complex and the removal of unfavorable bonds might be the main reason for the change of enzyme properties. In addition, the optimal temperature of the three mutants changed from 60 to 55 °C. These results indicate that the site 121 plays a critical role in the catalytic activity and enzymatic properties of chitosanase. To our knowledge, the results provide novel data on chitosanase activity and identify an excellent candidate of industrial chitosanase.

Using 1-((6-chloropydidin-3-yl)methyl)-7-methyl-8-nitro-5propoxy-1,2,3,5,6,7-hexahydroimidazo[1,2-α-]-pyridine (IPP) as the sole carbon source, we isolated a strain with a higher activity of IPP-degrading bacterium Sphingobacterium sp. P1-3 from soil. At 30 °C, pH 7.0 ,and 10 mg L(-1) IPP content, the degradation rate of IPP by Sphingobacterium sp. P1-3 could reach 57.75 and 62.47% in 20 and 30 days, respectively. The value of DT50 of IPP was 27 d at the level of 30 mg L(-1) IPP, while DT50 in the blank test was 151 d. During the IPP biodegradation process, five intermediates (M1-M5) were monitored and identified. On the basis of the identified metabolites and their biodegradation courses, a possible biodegradation pathway was proposed. IPP biodegradation mainly occurred on the tetrahydropyridine ring. IPP was transformed to five different metabolites by strain P1-3 through the oxidation and elimination of methyl, propyl, and nitro groups. Moreover, a new pathway involving M2 (1-((6-chloropydidin-3-yl)methyl)-7-methyl-8-hydroxy-5-propoxy-1,2,3,5,6,7-hexahydroimidazo [1,2-α-]-pyridine), M3 (1-((6-chloropydidin-3-yl)methyl)-7-methyl-5-carbonyl-1,2,3,5,6,7-hexahydroimidazo[1,2-α-]-pyridine), and M5 (8-amino-1,2,3,5,6,7-hexahydroimidazo[1,2-α-]-pyridine) was first monitored and identified.