Zhi-Liang Zhang

Preparation and application of chitosan nanoparticles and nanofibers

Encapsulation and immobilization technology is important for the food processing and bioengineering industries. Chitosan is a natural polysaccharide prepared by the N - deacetylation of chitin. It has been widely used in food and bioengineering industries, including the encapsulation of active food ingredients, in enzyme immobilization, and as a carrier for controlled drug delivery, due to its significant biological and chemical properties such as biodegradability, biocompatibility, bioactivity, and polycationicity. In this work, chitosan nanoparticles and nanofibers used to encapsulate bioactive substances and immobilize enzymes were reviewed. Preparation of chitosan nanoparticles and nanofibers, including the work achieved in our group on chitosan nanoparticles for enzyme immobilization, were also introduced. Some problems encountered with nano - structured chitosan carriers for bioactive substance encapsulation and enzyme immobilization were discussed, together with the future prospects of such systems.

NANOSIZE MgO AS ANTIBACTERIAL AGENT: PREPARATION AND CHARACTERISTICS

The antibacterial activity of MgO nanoparticles prepared by a sonication method was evaluated in this paper. The effect of calcination conditions on the size and antibacterial activity of MgO nanoparticles was investigated. MgO nanoparticles were characterized for purity (TGA), crystallinity and crystal size (XRD), particle size and morphology (TEM) and surface area (BET). Results showed that the smallest size of 6 nm could be obtained. The lethal effects of nanocrystalline MgO were evaluated on Lactobacillus plantarum. At a concentration of 100 ppm, the killing effect of MgO was close to 1 log reduction for L. plantarum after 24 h exposure. At 1000 ppm and 24 h exposure, the killing effect of MgO was more than a 2.8 log reduction. With the increase of calcination time, the lethal effect of MgO nanoparticles increased after 6 h or 24 h exposure at 100 ppm or 1000 ppm. 2.86 log and 2.89 log were killed at 1000 ppm after 24 h exposure using the sample MgO, sonication, A, and the sample MgO, sonication, B, respectively. When the sample MgO, sonication, C, was used, the lethal quantity of L. plantarum was increased to a 3.36 log reduction.

Sonication-assisted preparation of CaO nanoparticles for antibacterial agents

The effect of calcination conditions on the size and killing activity of CaO nanoparticles towards L. plantarum was studied in this paper. The results showed that CaO nanoparticles with a diameter of 20 nm could be obtained under the investigated conditions. The lethal effect of CaO nanoparticles after incubation of 6 or 24 h increased with increasing calcination time. Using CaO-SA, CaO-SB, and CaO-SC after a 24-h exposure, 2.25, 3.37, and 5.97 log L. plantarum were killed, respectively, at a concentration of 100 ppm. The current results show that the use of CaO nanoparticles as antibacterial agents has significant potential in food-relevant industries.

Production of a new non-specific nuclease from Yersinia enterocolitica subsp. palearctica: optimization of induction conditions using response surface methodology.

A new non-specific nuclease from Yersinia enterocolitica subsp. palearctica (Y. NSN) was expressed in Escherichia coli (E. coli) BL 21 StarTM (DE3)plysS. Induction conditions, including isopropyl-β-D-thiogalactoside (IPTG) concentration, cell density (OD600), induction time and induction temperature, were optimized using response surface methodology. Statistical analysis of the results revealed that induction temperature and all the quadratic terms of variables had significant effects on enzyme activity of Y. NSN. The optimal induction conditions were as follows: 1.5 mmol/L IPTG, OD600 of 0.80, induction time of 20.5 h, and induction temperature of 32 °C. Under the optimized conditions, the highest enzyme activity could be obtained.

Research Article: Bioinformatics analysis of a non-specific nuclease from Yersinia enterocolitica subsp. palearctica

In this paper, the physical and chemical characteristics, biological structure and function of a non-specific nuclease from Yersinia enterocolitica subsp. palearctica (Y. NSN) found in our group were studied using multiple bioinformatics approaches. The results showed that Y. NSN had 283 amino acids, a weight of 30,692.5 ku and a certain hydrophilic property. Y. NSN had a signal peptide, no transmembrane domains and disulphide bonds. Cleavage site in Y. NSN was between pos. 23 and 24. The prediction result of the secondary structure showed Y. NSN was a coil structure-based protein. The ratio of α-helix, β-folded and random coil were 18.73%, 16.96% and 64.31%, respectively. Active sites were pos. 124, 125, 127, 157, 165 and 169. Mg(2+) binding site was pos. 157. Substrate binding sites were pos. 124, 125 and 169. The analysis of multisequencing alignment and phylogenetic tree indicated that Y. NSN shared high similarity with the nuclease from Y. enterocolitica subsp. enterocolitica 8081. The enzyme activity results showed that Y. NSN was a nuclease with good thermostability.