Biomedical subjects

Mingcheng Zhang

Publications and source records attributed to Mingcheng Zhang.

5 recordsLinked to original sources

PubMed2026

Applications of metal-organic frameworks in smart packaging for food freshness indication: a comprehensive review.

Smart packaging is extensively studied for its multifunctional capabilities in antimicrobial activity, preservation, and atmosphere modification. Recently emerged metal-organic frameworks (MOFs) freshness-indicating packaging becomes a key research direction in smart packaging owing to its distinctive functions and physicochemical properties. As multifunctional materials, the unique porous structure and tunable properties of MOFs provide a distinctive approach for developing food packaging applications dedicated to food freshness indication. Existing MOFs-based smart packaging still faces potential safety risks and technical challenges in practical applications, and there remains a lack of integrated discussion that combines synthesis strategies, packaging design, optimization, and safety assessment. This review elaborates on the application of MOFs in freshness-indicating smart packaging, focusing on diverse MOFs synthesis strategies, the formats of smart packaging, types of indicator signals, and qualitative/quantitative analytical methods. It also delves into the methodology concepts of MOFs-based smart packaging and evaluates MOFs safety in food packaging by addressing potential risks. Studies show that MOFs-based smart packaging achieves qualitative and semi-quantitative analysis of food freshness through multiple signal modalities such as visible color change, fluorescence, and photothermal effects. This review emphasizes that safe MOFs design is critically important and should comply with the overall migration limit of <10 mg/dm2 specified in Regulation (EC) No 1935/2004, lanthanide element limit of <0.05 mg/kg, and FDA threshold of 1.5 μg/person/day. Comprehensive safety assessment and intelligent sensing platforms will constitute pivotal directions for advancing MOFs-based smart packaging toward practical application.

Food Packaging↗

PubMed2002

[Expression of thermal stable, soluble hepatitis E virus recombinant antigen].

BACKGROUND: To obtain thermal stable, soluble, biologically active hepatitis E virus recombinant antigen using thioredoxin fusion expression system. METHODS: HEV ORF2 gene fragment (6964-7126 nt) was inserted into thioredoxin fusion expression vector pThioHisA. The recombinant plasmid was transformed into E. coli BL21 strain. After induction with IPTG, cells were lysed and the supernatant was subjected to 80 degree treatment for 10 minutes. After centrifugation, the supernatant was tested by ELISA. RESULTS: SDS-PAGE analysis showed the thioredoxin. HEV fusion protein was highly expressed and was thermally stable, soluble. HEV specific ELISA confirmed this fusion protein possessing HEV specific antigenicity. CONCLUSIONS: Using thioredoxin fusion expression system, a soluble, thermal stable, biologically active HEV recombinant antigen was successfully expressed.

Antigens, Viral↗

PubMed2002

[Preliminary evidence that a hepatitis E virus (HEV) ORF2 recombinant protein protects cynomolgus macaques against challenge with wild-type HEV].

BACKGROUND: To observe the protective effect of hepatitis E virus (HEV) ORF2 recombinant protein expressed in prokaryote cell cynomolgus macaques (cynos) against challenging with wild-type HEV. METHODS: Cynos were immunized with HEV ORF2 recombinant protein and then challenged with wild-type HEV, the unimmunized cynos were used as control. Blood samples were collected and tested to see if there were dynamic changes of ALT and antibody to HEV before and after challenge with wild-type HEV. RESULTS: All the five unimmunized cynos re-presented hepatitis 3 weeks after challenging with wild-type HEV. However, all the five immunized cynos showed no hepatitis and pathological changes. CONCLUSIONS: Cynos can be efficiently protected by immunization with HEV ORF2 recombinant protein against wild-type HEV. This protein can be a promising candidate for HEV vaccine.

Animals↗

PubMed2002

[Cloning and expression of simplex herpes virus ? US4 fragment].

BACKGROUND: To get early laboratory study of type specific antigenicity of herpes simplex virus II. METHODS: PCR and prokaryotic expression technique. RESULTS: Herpes simplex virus II type specific gene fragment was expressed in E.coli and the products can be used as specific antigen for the detection of anti\HSV in the recovery sera. CONCLUSIONS: Cloning and express of HSVII type specific antigen found the basis for developing specific diagnosis methods and vaccine of HSV.

Antigens, Viral↗

PubMed2002

[Expression of full-length hepatitis E virus structural gene using baculovirus expression system].

OBJECTIVE: To obtain recombinant baculovirus containing full-length structural gene of HEV and to express HEV structural protein. METHODS: Full-length structural gene of HEV (5147-7126 nt) was inserted into baculovirus expression vector pAcUW51. The recombinant plasmid and Baculo Gold DNA were co-transfected into insect cell line Sf9. Single plaque was picked and amplified and expression of HEV structural protein was tested by SDS-PAGE, Western blot and immunofluorescence methods. RESULTS: SDS-PAGE analysis showed HEV structural protein was highly expressed; Western blot and immunofluorescence assay showed that the expression product could specifically react with HEV positive sera, confirming the protein possessing HEV specific antigenicity. CONCLUSIONS: HEV structural protein was successfully expressed using baculovirus expression system.

Animals↗