Development of a sequential injection analysis system for monitoring of trehalose concentrations

Rhee, Jong Il

doi:10.1007/bf02931106

Cited by 6 publications

(4 citation statements)

References 21 publications

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“…The absorbance was measured at 405 nm by a UV/Vis spectrophotometer (Multiskan Spectrum, Thermo Co., Vantaa, Finland) with a flow-through cell (inner volume of 100 μL, optical path length of 10 mm, Hellma GmbH, Muelheim, Germany). The control of the SIA system and its operating sequence is almost the same as that described in the reference [27].…”

Section: Sequential Injection Analysis (Sia) System For Glucose Monitmentioning

confidence: 95%

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Immobilization of glucose oxidase and lactate dehydrogenase onto magnetic nanoparticles for bioprocess monitoring system

Sohn

Kim

Rhee

2008

Biotechnol Bioproc E

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Glucose oxidase (GOD) and lactate dehydrogenase (LDH) were immobilized onto magnetic nanoparticles, viz. Fe 3 O 4 , via carbodiimide and glutaraldehyde. The immobilization efficiency was largely dependent upon the immobilization time and concentration of glutaraldehyde. The magnetic nanoparticles had a mean diameter of 9.3 nm and were superparamagnetic. The immobilization of GOD and LDH on the nanoparticles slightly decreased their saturation magnetization. However, the FT-IR spectra showed that GOD and LDH were immobilized onto the nanoparticles by different binding mechanisms, the reason for which was not well explained. The optimum pH values of the immobilized GOD and LDH were changed to 8 and 10, respectively. The free and immobilized enzyme kinetic parameters (K m and V max ) were determined by Michaelis-Menten enzyme kinetics. The K m values for free and immobilized GOD were 0.168 and 0.324 mM, respectively, while those for free and immobilized LDH were 0.19 and 0.163 mM for NAD, and 2.976 and 4.785 mM for lactate, respectively. High operational stability was observed, with more than 80% of the initial enzyme activity being retained for the immobilized GOD up to 12 h and for the immobilized LDH up to 24 h. The immobilized GOD was applied to a sequential injection analysis system for the application of bioprocess monitoring. © KSBB

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Section: Sequential Injection Analysis (Sia) System For Glucose Monitmentioning

confidence: 95%

“…: 4 mm, length: 20 mm) placed G over a permanent magnet and then integrated into a sequential injection system described in the references [26,27]. Samples (50 μL) and reagents [0.5 mL of ABTS (10 mM) and 0.3 mL of HRP (100 U/mL)] were injected into the half packed silicon tube sequentially.…”

Section: Sequential Injection Analysis (Sia) System For Glucose Monitmentioning

confidence: 99%

Immobilization of glucose oxidase and lactate dehydrogenase onto magnetic nanoparticles for bioprocess monitoring system

Sohn

Kim

Rhee

2008

Biotechnol Bioproc E

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“…Afterwards, the selection valve is switched to the outlet port (here position 5), and the segments are propelled forward towards the detector, undergoing on their way dispersion and thereby partial mixing with each other, and hence promoting chemical reaction, the result of which is monitored by the detector. Notable advantages of SI as compared to FI are in particular that it allows the exact metering of even smaller volumetric volumes (of the order of a few microlitres), which fostered the use of liquid enzymes (49,50) and costly cofactors as demanded in NAD-linked enzymic assays (40). Further, thanks to the use of a syringe pump, SI is much better suited for stopped-flow procedures where a very precisely selected delay time is necessary, and that it readily and reproducibly permits flow reversals, which, in fact, in addition as a mere means of transport, also might be used to promote mixing of sample and reagent(s) and facilitate controlled sample dilution within the HC.…”

Section: X5 Fundamentals Of Sequential Injection Analysismentioning

confidence: 99%

Flow Injection Analysis in Industrial Biotechnology

Hansen

Miró

2009

Encyclopedia of Industrial Biotechnology

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Flow injection analysis (FIA) is an analytical chemical continuous flow (CF) method which, in contrast to traditional CF procedures, does not rely on complete physical mixing (homogenization) of the sample and the reagent(s) or on attaining chemical equilibria of the chemical reactions involved. Exploiting controllable dispersion of the injected sample within the reagent‐containing carrier stream and strictly reproducible timing of all events taking place, it is based on measuring transient signals, which not only implies very high sampling rates but also, and most importantly, permits implementation of a number of novel methodologies that are not feasible when performed under batch conditions or by conventional CF procedures. Demonstrated for selected bioanalytical and technological applications encompassing cellular and enzymatic assays as well as monitoring of culture media, the principles and operational characteristics of FIA are first outlined, and then its downscaled/miniaturized sequels, that is, sequential injection analysis (SIA) and lab‐on‐valve (LOV), are detailed. Thus, in SIA the sample and reagents are, via the use of a multi‐position valve and an attached syringe pump operated under full programmable control, aspirated sequentially and then propelled forward allowing the sample and reagent(s) to be intermixed and, if called for, subjected to appropriate treatments before analyte detection. This infers that, merely minute sample/reagent volumes are consumed, hence leading to generation of small amounts of waste. In LOV this downscaling is taken further by using a small monolithic structure within which all sample manipulations and ultimate analyte detection under programmable control can be effected. Even bead materials with different surface groups/characteristics, including live cells, can be handled and utilized as demonstrated. Because the syringe pump in SIA and LOV can be used for accurately aspirating, propelling or even stopping the flow, these modi operandi allow fully to exploit the interplay between the kinetics and the thermodynamics of the chemical reactions involved, so that there are no restrictions whatsoever as to the chemistries that can be implemented, even if they entail multistep reactions. Representative bioanalytical examples of this interplay are presented.

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“…For applications using this coupling reaction, a lot of studies have developed the utilization of glucose oxidase and HRP in detection and monitoring of glucose level in many platforms, e.g., the determination of glucose in serum samples with Sol-Gel matrix (El-Essi et al, 1997;Lan et al, 2008) or multicolor biosensor(Lin et al, 2016), an electrochemical biosensor for glucose measurement in beverages(Yabuki et al, 2001), and in vivo on-line monitoring tool of glucose in rabbit blood(Li et al, 2001). Besides glucose, these coupling enzymes have also been used with other carbohydrate-metabolizing enzymes or glycosidases for determination of other sugars and glycosides, e.g., lactose(Condezo-Hoyos et al, 2014;Eshkenazi et al, 2000), trehalose(Il Rhee et al, 2007), sucrose and fructose (Aksorn and Teepoo, 2020) and stevioside(Udompaisarn et al, 2017;Boonkaew et al, 2019). Moreover, HRP has been used in the development of enzymatic sensors for detection and monitoring of various substances, as well as in other areas of immunoassays, histochemistry, wastewater treatment, organic compounds synthesis, and biomedical applications(Azevedo et al, 2003).…”

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confidence: 99%

Cassava Root Cortex Peroxidase (CCP) as a Potential Alternative Source of Peroxidase

Sornwatana

Rotchanapreeda

Wongsamart

et al. 2022

Preprint

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Cassava is one of the most important starch crops in the world. Cassava starch factories normally generate a huge amount of cassava tuberous root residual which is usually discarded and might cause pollution to the environment. In order to find some extra benefits of such waste, in this study, cassava root cortex peroxidase (CCP) was found up to 20 mg/kg fresh deteriorated cortex tissue from tuberous root and also able to demonstrate some applications similar to horseradish peroxidase (HRP). The characterization revealed that major native CCP was a 105-kDa dimeric peroxidase with two 54-kDa monomers. Using 3,3′-diaminobenzidine (DAB) as substrate in the assay, CCP was found to be tolerant and could maintain its activity in a wide temperature range from 20 to 70°C with an optimum at 65°C. CCP was stable in board pH range from 3 to 11 with maximum activity at pH 5.0. Despite simple purification with ammonium sulfate precipitation, partial purified CCP was capable of determining glucose concentrations with glucose oxidase as similar capability as horseradish peroxidase (HRP). For application as reporter enzyme in immunoassays, the self-made secondary antibody conjugated with CCP did successfully detect the protein antigen in Western blot analysis using the luminol as chemiluminescent substrate. These demonstrations indicated CCP as one of the most robust peroxidases. Moreover, the active enzyme could be easily retrieved from the industrial waste of cassava peel at low cost. Further studies should involve optimization of enzyme purification in industrial scale and finding more CCP potential applications which should increase the advantages of this promising enzyme.

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Development of a sequential injection analysis system for monitoring of trehalose concentrations

Cited by 6 publications

References 21 publications

Immobilization of glucose oxidase and lactate dehydrogenase onto magnetic nanoparticles for bioprocess monitoring system

Immobilization of glucose oxidase and lactate dehydrogenase onto magnetic nanoparticles for bioprocess monitoring system

Flow Injection Analysis in Industrial Biotechnology

Cassava Root Cortex Peroxidase (CCP) as a Potential Alternative Source of Peroxidase

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