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Biochemical Engineering Journal (v.72, #)
Stabilization of semi-solid-state starch by branching enzyme-assisted chain-transfer catalysis at extreme substrate concentration by Susanne L. Jensen; Flemming H. Larsen; Ole Bandsholm; Andreas Blennow (pp. 1-10).
Display Omitted► A branching enzyme was used to modify thermally partially opened starch granules. ► Highly branched, molecularly uniform and cross-linked granular starch was generated. ► A new concept for enzyme-assisted modification of compact polysaccharides is provided.In this study a branching enzyme (BE, α-1,4→α-1,6 glycosyltransferase) was used to modify starch granules of different structures at high temperature and at extreme starch dry matter content (30–40%, w/v) to restrict temperature-induced swelling. As opposed to diluted systems, such conditions led to stabilization of the granular structure for low-phosphate starch types at the highest BE activity. Bright field/polarized light and scanning electron microscopy confirmed maintenance of granular structure. The product compared to the control had significantly increased degree of branching as identified by shorter branch-length of the α-1,4 chains assessed by chromatography and larger proportion of α-1,6 links to α-1,4 links as assessed by1H nuclear magnetic resonance spectroscopy. Size exclusion chromatography demonstrated the presence of uniform molecules with smaller size. Further the polysaccharide product was 40% more soluble at 25°C than the corresponding heat treated control. Both of these observations were supported by13C solid-state MAS NMR. Hence, significant chain transfer took place in the semi-solid state starch permitting conservation of the main granular organization in the final product. A hypothetic model is presented to account for the observed phenomenon.
Keywords: Abbreviations; AP; amylopectin; AM; amylose; BE; branching enzyme; BEU; branching enzyme unit; CBM; carbohydrate binding module; CP; cross polarization; DM; dry matter; GWD; glucan water dikinase; HPAEC-PAD; high performance anion exchange chromatography with pulsed amperometric detection; HR; high resolution; MAS; magic angle spinning; NMR; nuclear magnetic resonance; SEC; size exclusion chromatography; SEM; scanning electron microscopy; S/N; signal to noise; SP; single pulseStarch; Biocatalysis; Enzyme technology; Heterogeneous reaction; Branching enzyme; Raw starch modification
Stability and catalytic kinetics of protease loaded liposomes by Zahra Vafabakhsh; Kianoush Khosravi-Darani; Khosro Khajeh; Mahshid Jahadi; Rozita Komeili; Amir Mohammad Mortazavian (pp. 11-17).
► Liposomes prepared by Mozafari method were used for encapsulation of Flavourzyme. ► Kinetic parameters of free and encapsulated Flavourzyme were compared. ► Optimum incubation condition and stability of encapsulated enzyme were studied. ► Proteolysis trend in recombined milk containing enzyme was comprised. ► A gradually fulfilling proteolysis of casein by liposomal enzyme was observed.The purpose of this study was to prepare liposomes through Mozafari method to encapsulate Flavourzyme as the flavor-enhancing enzyme at cheese ripening. Some kinetic parameters of encapsulated protease were determined and compared with corresponding free enzyme. Kinetic studies indicated an increase in both Michaelis–Menten constant and maximum velocity in encapsulated Flavourzyme. Optimum incubation temperature and pH of encapsulated enzyme did not show any significant difference with the free one. Evaluation of the thermal stability (at 35, 45 and 55°C) shows that encapsulated enzyme was stable at 35°C during in 6h. Also decreased stability of encapsulated enzyme has been observed at 65 and 75°C in 1h. The results show increase of stability of encapsulated enzymes in pHs 7 and 8 (7h), while it was decreased in acidic condition. Results indicate the gradually fulfilling proteolysis of casein by liposomal loaded Flavourzyme in comparison with the free enzyme.
Keywords: Flavourzyme; Liposome; Mozafari method; Kinetic parameters; Proteolysis
Effect of different parameters on the hydrolytic activity of cross-linked enzyme aggregates (CLEAs) of lipase from Thermomyces lanuginosa by M.P. Guauque Torres; M.L. Foresti; M.L. Ferreira (pp. 18-23).
Display Omitted► CLEAs with BSA as cofeeder. ► Optimization of CLEAs synthesis. ► Additives do not increase recovered hydrolytic activity. ► Layered CLEAs synthesis successful.Cross-linked enzyme aggregates (CLEAs) of lipase from Thermomyces lanuginosa (TLL) were synthesized using (NH4)2SO4 as precipitant and glutaraldehyde as cross-linking agent. CLEAs were assayed for their hydrolytic activity in a reaction performed in an emulsioned medium. The effects of the amount of precipitant, cross-linker, and different additives such as protein cofeeder, oleic acid, n-heptane, sodium dodecyl sulfate (SDS), polyethylenglicol (PEG) and ethylendiamine were studied at selected ratios with respect to TLL mass. Traditional non-layered CLEAs of TLL showed recovered activities between 3 and 31% when compared with native lipase. Novel TLL layered CLEAs consisting of a protein cofeeder core and successive layers of target lipase showed an important increase in their retained activity. The highest recovered activity was found for the one-layered non-additivated CLEAs of TLL which showed a recovered activity of 75%.
Keywords: CLEA; Lipase; Layered CLEAs; Recovered activity
Direct ethanol production from N-acetylglucosamine and chitin substrates by Mucor species by Kentaro Inokuma; Maki Takano; Kazuhiro Hoshino (pp. 24-32).
► We evaluate ethanol production capacity of Mucor strains from GlcNAc and chitin. ► Wide variety of Mucor strains produce ethanol from GlcNAc efficiently. ► Some Mucor strains directly convert colloidal chitin into ethanol.Chitin, which is a polymer of β-(1–4) linked N-acetyl-d-glucosamine (GlcNAc) residues, is one of the most abundant renewable resources in nature, after cellulose. In this study, we found some native Mucor strains, which can use GlcNAc and chitin substrates as carbon sources for growth and ethanol production. One of these strains, M. circinelloides NBRC 6746 produced 18.6±0.6g/l of ethanol from 50g/l of GlcNAc after 72h and the maximum ethanol production rate was 0.75±0.1g/l/h. Furthermore, M. circinelloides NBRC 4572 produced 6.00±0.22 and 0.46±0.04g/l of ethanol from 50g/l of colloidal chitin and chitin powder after 16 and 12 days, respectively. We also found an extracellular chitinolytic enzyme producing strain M. ambiguus NBRC 8092, and successfully improved ethanol productivity of NBRC 4572 from colloidal chitin using crude chitinolytic enzyme derived from NBRC 8092. The ethanol titer reached 9.44±0.10g/l after 16 days. These results were the first bioethanol production from GlcNAc and chitin substrates by native organisms, and also suggest that these Mucor strains have great potential for the simultaneous saccharification and fermentation (SSF) of chitin biomass.
Keywords: Ethanol; N; -acetylglucosamine; Chitin; Bioconversion; Biodegradation; Fermentation
Purification of transgenic tobacco-derived recombinant human monoclonal antibody by Mukesh Mayani; Carlos D.M. Filipe; Michael D. McLean; J. Christopher Hall; Raja Ghosh (pp. 33-41).
► Efficient purification of transgenic monoclonal antibody. ► Use of cascade ultrafiltration as a pre-enrichment technique. ► 97% impurities removal and almost complete antibody recovery by ultrafiltration. ► Rational combination of ultrafiltration with chromatography. ► Greater than 95% purity with 50% overall recovery.Purification of recombinant monoclonal antibody from transgenic plant extract is technically challenging as it involves the processing of large volume of material, containing low titre of antibody, present along with large quantities of native proteins and other impurities. The conventional approach of capturing antibody from a clarified extract using packed-bed chromatography is therefore not particularly suitable. This study evaluates the suitability of using a combination of ultrafiltration and chromatography for purifying transgenic tobacco-derived human monoclonal antibody. A two-stage cascade ultrafiltration process removed about 97% impurities while ensuring almost complete recovery of antibody, providing 32-fold antibody enrichment in the process. The primary objective of the ultrafiltration step was to reduce the burden on the subsequent chromatographic steps. A two-step chromatographic process was then used to eliminate remaining impurities. Using this approach, recombinant human antibody expressed in tobacco could be purified to greater than 95% purity with 50% overall recovery (ca. 12.5mgantibody/kg tobacco tissues).
Keywords: Monoclonal antibody; Transgenic tobacco; Purification; Ultrafiltration; Chromatography
Enhanced production of CoQ10 by constitutive overexpression of 3-demethyl ubiquinone-9 3-methyltransferase under tac promoter in Rhodobacter sphaeroides by Wenqiang Lu; Yijun Shi; Shuaiwei He; Yunzhou Fei; Kai Yu; Hongwei Yu (pp. 42-47).
► A constitutive expression vector based on tac promoter was developed. ► Overexpression of UbiG in Rhodobacter sphaeroides improved the production of CoQ10. ► IPTG had negative effect on the CoQ10 production of R. sphaeroides. ► Engineering the CoQ10 biosynthetic pathway in membrane-rich host is more effective.Coenzyme Q10 (CoQ10), as an essential electron carrier in the aerobic respiratory electron transfer system, has been proven to be an effective compound in health care and disease prevention. With the aim of improving the production of CoQ10, the biosynthetic pathway of CoQ10 was engineered in Rhodobacter sphaeroides by overexpressing 3-demethyl ubiquinone-9 3-methyltransferase (UbiG), which catalyzes the two steps of O-methylations of the quinonoid ring. For expressing the UbiG, a constitutive expression vector harboring tac promoter and ubiG gene was firstly developed. After cultivated in dark conditions, the transcriptional level of ubiG of the recombinant R. sphaeroides without inducer, which approached to that of with inducer, was about 133 times that of the wild type. The production was correspondingly improved up to 65.8mg/L compared to 47.6mg/L for the wild type. In addition, it was found that isopropyl-beta-d-thiogalactopyranoside (IPTG) had a negative effect on CoQ10 production when added to the medium, although it showed no significant influence on the growth rate of the microbes.
Keywords: Abbreviations; UbiG; 3-demethyl ubiquinone-9 3-methyltransferase; CoQ; 10; coenzyme Q; 10; R. sphaeroides; Rhodobacter sphaeroides; E. coli; Escherichia coli; DCW; dry cell weight; IPTG; isopropyl-beta-; d; -thiogalactopyranosideMetabolite over production; Biosynthesis; Enzymes; Microbial growth; Coenzyme Q; 10; 3-Demethyl ubiquinone-9 3-methyltransferase
Biotreatment of heavy oil wastewater by combined upflow anaerobic sludge blanket and immobilized biological aerated filter in a pilot-scale test by Guo-hua Liu; Zhengfang Ye; Kun Tong; Yi-he Zhang (pp. 48-53).
► Heavy oil wastewater was treated by a pilot combined bioreactor. ► The COD, NH3-N and SS in the wastewater can be removed effectively. ► Most of alkanes can be degraded in a UASB process. ► Immobilized-BAF plays an important role for removing the NH3-N and SS. ► Bacterial species belonging to Bacillales and Rhodobacterales were alkane-degraders.A field pilot study has been constructed in the Liaohe oilfield, China to treat heavy oil wastewater with large amounts of dissolved recalcitrant organic compounds and low nutrient of nitrogen and phosphorus by an upflow anaerobic sludge blanket (UASB) coupled with immobilized biological aerated filters (I-BAFs). By operating the system for 252 days (including the start-up of 128 days), the chemical oxygen demand (COD), ammonia nitrogen (NH3-N) and suspended solid (SS) in the wastewater were removed by 74%, 94% and 98%, respectively. GC–MS analysis indicated that most of alkanes were degraded by the UASB process, while the I-BAF played important roles both in degrading organic compounds and in removing the NH3-N and SS. The bacterial community structural analysis based on the PCR-DGGE technology reveals that the predominant bacteria in the UASB reactor belong to the Bacillales and Rhodobacterales, and that in the I-BAF was identified as uncultured soil bacterium. Our results suggest that the combined biotreatment system has immense potential in large-scale treatment of heavy oil wastewater.
Keywords: Heavy oil wastewater; Biodegradation; Anaerobic processes; Immobilized cells; GC–MS; DNA
Biotransformation of indole by whole cells of recombinant biphenyl dioxygenase and biphenyl-2,3-dihydrodiol-2,3-dehydrogenase by Yuanyuan Qu; Bingwen Xu; Xuwang Zhang; Qiao Ma; Hao Zhou; Chunlei Kong; Zhaojing Zhang; Jiti Zhou (pp. 54-60).
► The bphAB genes were cloned from Dyella ginsengisoli LA-4 and expressed in Escherichia coli. ► The feasibility of indole transformation was predicted by molecular docking studies. ► A maximum indigo yield of 44mg/L was produced from 200mg/L indole. ► The products during indole transformation were identified by HPLC–MS. ► The pathway of indole transformation by strain AB_IND was proposed.The introduction of hydroxyl groups into indole molecule by different mono- and dioxygenases leads to the production of indigo. As a well-known biocatalyst, biphenyl dioxygenase possessed the ability to transform indole to indigo. However, there has been little information about this enzymatic transformation process. In this study, the genes encoding biphenyl dioxygenase (BphA) and biphenyl-2,3-dihydrodiol 2,3-dehydrogenase (BphB) were cloned from Dyella ginsengisoli LA-4 and heterologously expressed in Escherichia coli (DE3) (designated as AB_IND). The feasibility of indole transformation to indigo by strain BphA_LA-4 was predicted by molecular docking studies. The biotransformation ratios of indole (100mg/L) reached the maximum (95%) when cells were induced at 15°C with 0.25mM IPTG in M9 medium. In addition, 44mg/L indigo was produced from 200mg/L indole when supplied with 0.28g/L of biomass and 0.2% (w/v) glucose. HPLC–MS was used to identify the products, which showed that indigo was the major product. Meanwhile, indirubin and isatin were also identified during the transformation process. Furthermore, the pathway of indole transformation by strain AB_IND was also proposed.
Keywords: Biotransformation; Biphenyl dioxygenase; Indole; Indigo; Molecular docking
Unmarked insertional inactivation in the gfo gene improves growth and ethanol production by Zymomonas mobilis ZM4 in sucrose without formation of sorbitol as a by-product, but yields opposite effects in high glucose by Cui Wang; Cheng Liu; Jiefang Hong; Kun Zhang; Yuanyuan Ma; Shaolan Zou; Minhua Zhang (pp. 61-69).
► An unmarked gfo mutant from Zymomonas mobilis ZM4 was constructed. ► gfo inactivation improved growth and ethanol production in 1M (342g/L) sucrose. ► gfo inactivation impaired growth and ethanol production in 1.11M (200g/L) glucose. ► Sorbitol accelerated growth and sucrose hydrolysis by the mutant in 1M sucrose. ► Sorbitol restored growth and ethanol production by the mutant in 1.11M glucose.Sorbitol, one of the main by-products of growth on high sucrose concentrations, is catalyzed by glucose-fructose oxidoreductase (GFOR, EC 1.1.99.28) in Zymomonas mobilis, which decreases the ethanol yield. In this study, an unmarked gfo mutant from Z. mobilis ZM4 was constructed using a site-specific FLP recombinase, and growth and ethanol production were evaluated with or without the addition of sorbitol to the media. The inactivation of gfo had contrasting effects in different substrates, especially at high concentrations. The maximum specific growth rate ( μm) and theoretical ethanol yield value ( Ym) increased from 0.065h−1 and 60.56% to 0.094h−1 and 83.87% in 342g/L sucrose, respectively. Conversely, in 200g/L glucose, gfo inactivation decreased μm and Ym from 0.15h−1 and 89.85% to 0.10h−1 and 67.59%, respectively, and prolonged the lag period from 16h to 40h. The addition of sorbitol slightly accelerated growth and sucrose hydrolysis by the gfo mutant in 342g/L sucrose; however, addition of sorbitol restored the μm and Ym of the gfo mutant in 200g/L glucose to 0.14h−1 and 82.50%, respectively. Inactivation of gfo had a small effect on fructose utilization, and a positive one on mixture of glucose and fructose similar to that on sucrose. These results provide further understanding of the osmoregulation mechanisms in Z. mobilis and may help to exploit the biotechnological applications of this industrially important bacterium.
Keywords: Zymomonas mobilis; Glucose-fructose oxidoreductase inactivation; Sucrose; Glucose; Growth; Ethanol production
Characterization of a laccase-like multicopper oxidase from newly isolated Streptomyces sp. C1 in agricultural waste compost and enzymatic decolorization of azo dyes by Lunhui Lu; Guangming Zeng; Changzheng Fan; Xiujuan Ren; Cong Wang; Qianru Zhao; Jiachao Zhang; Ming Chen; Anwei Chen; Min Jiang (pp. 70-76).
► A newly laccase-producing Streptomyces sp. C1 was screened out from composting. ► We characterized a alkali-tolerant and moderately thermostable LMCO from strain C1. ► This two-domain LMCO had specific characteristics like other Streptomyces LMCOs. ► Results showed importance of Streptomyces in lignin decomposition during composting.Laccases or laccase-like multicopper oxidases (LMCOs) could catalyze the oxidation of various substrates coupled to the reduction of oxygen to water. In this study, eight strains with laccase activity were isolated from composting samples in different phases, among which strain C1 isolated from the thermophilic-phase sample presented the highest laccase activity. The purified LMCO of strain C1 showed a single protein band on SDS-PAGE gel with a molecular mass of about 38kDa. The novel laccase showed alkaline resistance and moderate thermostability. The enzyme activity was activated by some metal ions such as Cu2+, Co2+ and Fe3+ at the concentration of 1mM, while was strongly inhibited in the presence of Hg2+. The LMCO could efficiently decolorize the indigo carmine and diamond black PV with syringaldehyde as mediator, which suggested a great potential for dye decolorization in the textile industry. The novel strain was identified as Streptomyces sp. C1. The finding of new laccase-producing Streptomyces sp. C1 in this study will also contribute to the further explanation of the function of Actinomycetes in the thermophilic phase of composting.
Keywords: Lignin; Biodegradation; Waste treatment; Characterization; Laccase-like multicopper oxidase (LMCO); Enzyme activity
Biological detoxification of furfural and 5-hydroxyl methyl furfural in hydrolysate of oil palm empty fruit bunch by Enterobacter sp. FDS8 by Dongxu Zhang; Yee Ling Ong; Zhi Li; Jin Chuan Wu (pp. 77-82).
► Biological degradation of furfural and 5-hydroxy methyl furfural (HMF) by an new isolate. ► The highest biodegradation rates of furfural and HMF ever reported. ► Recycle and reuse of whole cells of the new isolates for at least 5 times without losing biodegradation efficiency.Biological detoxification of furfural and 5-hydroxyl methyl furfural (HMF) from lignocellulose hydrolysate is commercially attractive, but the lower process efficiency limits its practical applications. Highly efficient detoxification of furfural and HMF was developed by simply adding the whole cells of a newly isolated Enterobacter sp. FDS8 without the requirement of adding anything else, giving furfural and HMF degradation rates of up to 0.54gL−1h−1 and 0.12gL−1h−1, respectively, which are the highest biodetoxification rates ever reported, with a total sugar loss of below 5%. The whole cells were able to be recycled and reused for at least 5 times without losing their detoxification capability. When used for fermentation to produce lactic acid by Lactobacillus pentosus, the biologically detoxified oil palm empty fruit bunch (EFB) hydrolysate gave higher lactic acid productivity (1.7-fold), titer (1.5-fold) and yield (1.8-fold) compared to the un-detoxified EFB hydrolysate.
Keywords: Biological detoxification; Furfural; Hydroxy methyl furfural; Lignocellulose; Hydrolysate; Enterobacter; sp.
Purification and characterization of recombinant Bacillus subtilis 168 catalase using a basic polypeptide from ribosomal protein L2 by Junhuan Li; Yang Zhang; Haiying Chen; Yuntao Liu; Yanjun Yang (pp. 83-89).
► A basic polypeptide from protein L2 as an affinity tag was fused with catalase. ► Small ubiquitin-like modifier mediated tag removal method was adopted. ► The purification system for one-step purification yielded the catalase at greater than 95% purity. ► A high activity recovery of 74.5% was obtained by the above purification system.An efficient purification system for purifying recombinant Bacillus subtilis 168 catalase (KatA) expressed in Escherichia coli was developed. The basic region containing 252–273 amino acids derived from E. coli ribosomal protein L2 was used as an affinity tag while the small ubiquitin-like modifier (SUMO) was introduced as one specific protease cleavage site between the target protein and the purification tags. L2 (252–273)–SUMO fusion protein purification method can be effectively applied to purify the recombinant catalase using cation exchange resin. This purification procedure was used to purify the KatA and achieved a purification fold of 30.5, a specific activity of 48,227.2U/mg and an activity recovery of 74.5%. The enzyme showed a Soret peak at 407nm. The enzyme kept its activity between pH 5 and 10 and between 30°C and 60°C, with the highest activity at pH 8.0 and 37°C. The enzyme displayed an apparent Km of 39.08mM for hydrogen peroxide. These results agree well with the previous reports about B. subtilis catalase. L2 (252–273)–SUMO fusion protein purification technique provides a novel and effective fusion expression system for the production of recombinant proteins.
Keywords: Bioseparations; Chromatography; Downstream processing; Enzyme activity; Enzyme production; Ribosomal protein L2
Stepwise increase of spinosad production in Saccharopolyspora spinosa by metabolic engineering by Chaoyou Xue; Yuejiao Duan; Fanglong Zhao; Wenyu Lu (pp. 90-95).
► Unbalanced biosynthetic pathway of spinosad was stepwise is stepwise tuned. ► The yield of spinosad in the tuned Saccharopolyspora spinosa LU104 reached 405mg/L. ► We made a 5.0-fold enhancement of spinosad compared with wild-type S. spinosa.Rational metabolic and cellular engineering approaches are useful in improving strain performance. In the last years, several studies not only clarified the biosynthetic pathway of spinosad, but also provided useful information of metabolic restrictions in the spinosyn biosynthetic pathway. However, these studies overlooked the problem that the spinosyn biosynthetic pathway was unbalanced: the expression of six genes in the spinosyn biosynthetic pathway was insufficient; Saccharopolyspora spinosa accumulated useless compounds because of insufficient expression of SpnK. So a rational strain improvement strategy was developed to tune the unbalanced spinosyn biosynthetic pathway. First, we overexpressed spnK to increase the amount of the flux from rhamnosylated aglycone to pseudoaglycones (PSA). Then six genes ( spnP, spnO, spnN, spnQ, spnR, and spnS) involved in forosamine biosynthesis and spnK were co-expressed in S. spinosa LU102 to convert the accumulated PSA to spinosad. The yield of spinosad in S. spinosa LU102 was 214mg/L, which was 2.6-fold higher than that in the wild-type S. spinosa (82mg/L). Finally, spinosad production in the tuned S. spinosa LU104 was further increased to 405mg/L, which was a 5.0-fold enhancement compared with the wild-type S. spinosa, by duplicating spnP, spnO, spnN, spnQ, spnR, spnS, spnK, gtt, gdh and kre genes.
Keywords: Abbreviations; PSA; pseudoaglycones; R-AGL; rhamnosylated aglycone; FPP; farnesyl pyrophosphateBiosynthesis; Fermentation; Recombinant DNA; Enzymes; Tune; Spinosad
Co-immobilization of oxalate oxidase and catalase in films for scavenging of oxygen or oxalic acid by Sandra Winestrand; Kristin Johansson; Lars Järnström; Leif J. Jönsson (pp. 96-101).
► Highlights ► Oxalate oxidase and catalase were co-immobilized by entrapment. ► Immobilized oxalate oxidase can act as an oxygen or oxalic acid scavenger. ► Catalase prevented release of hydrogen peroxide from films with oxalate oxidase.Oxalate oxidase has potential to act as an oxygen scavenger in active packaging to increase the shelf-life of food and beverages, while simultaneously producing the protective packaging gas carbon dioxide. This study shows that oxalate oxidase from barley can be immobilized with retained catalytic activity through entrapment in a latex polymer matrix. Conditions for formation of film containing oxalate oxidase have been evaluated as well as effects of storage and latex on enzyme activity, migration of enzyme in films, and the ability of the latex films to resist higher temperatures. Drying of enzyme-containing latex films at 75°C prior to conditioning at 30°C resulted in higher activity than drying solely at 30°C, or drying at 95°C or 105°C followed by conditioning at 30°C. Storage of films in air at 4°C for 14 days did not negatively affect the enzymatic activity. Inclusion of catalase in films with oxalate oxidase effectively prevented release of hydrogen peroxide. The results suggest that the immobilized enzyme can successfully be used both as an oxygen scavenger and as an oxalic-acid scavenger.
Keywords: Oxalate oxidase; Active packaging; Oxygen scavenger; Oxalic acid; Latex; Entrapment
Apropos “A label-free immunosensor based on recordable compact disk chip for early diagnostic of the dengue virus infection” by Subhash C. Arya; Nirmala Agarwal (pp. 102-102).
Dengue; NS1 antigen; Immunosensor tests; Rapid tests; Field diagnosis; Laboratory support