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1.
Biosensors (Basel) ; 11(3)2021 Feb 25.
Article in English | MEDLINE | ID: mdl-33669087

ABSTRACT

Diabetes mellitus is a chronic metabolic disorder, being globally one of the most deadly diseases. This disease requires continually monitoring of the body's glucose levels. There are different types of sensors for measuring glucose, most of them invasive to the patient. Fiber optic sensors have been proven to have advantages compared to conventional sensors and they have great potential for various applications, especially in the biomedical area. Compared to other sensors, they are smaller, easy to handle, mostly non-invasive, thus leading to a lower risk of infection, high precision, well correlated and inexpensive. The objective of this review article is to compare different types of fiber optic sensors made with different experimental techniques applied to biomedicine, especially for glucose sensing. Observations are made on the way of elaboration, as well as the advantages and disadvantages that each one could have in real applications.


Subject(s)
Biosensing Techniques , Glucose/analysis , Fiber Optic Technology , Humans , Optical Fibers
2.
Molecules ; 20(10): 19372-92, 2015 Oct 23.
Article in English | MEDLINE | ID: mdl-26512637

ABSTRACT

ß-Glucosidase (EC 3.2.1.21) is a prominent member of the GH1 family of glycoside hydrolases. The properties of this ß-glucosidase appear to include resistance to temperature, urea, and iodoacetamide, and it is activated by 2-ME, similar to other members. ß-Glucosidase from chayote (Sechium edule) was purified by ionic-interchange chromatography and molecular exclusion chromatography. Peptides detected by LC-ESI-MS/MS were compared with other ß-glucosidases using the BLAST program. This enzyme is a 116 kDa protein composed of two sub-units of 58 kDa and shows homology with Cucumis sativus ß-glucosidase (NCBI reference sequence XP_004154617.1), in which seven peptides were found with relative masses ranging from 874.3643 to 1587.8297. The stability of ß-glucosidase depends on an initial concentration of 0.2 mg/mL of protein at pH 5.0 which decreases by 33% in a period of 30 h, and then stabilizes and is active for the next 5 days (pH 4.0 gives similar results). One hundred µg/mL ß-D-glucose inhibited ß-glucosidase activity by more than 50%. The enzyme had a Km of 4.88 mM with p-NPG and a Kcat of 10,000 min(-1). The optimal conditions for the enzyme require a pH of 4.0 and a temperature of 50 °C.


Subject(s)
Cucurbitaceae/enzymology , beta-Glucosidase/isolation & purification , Amino Acid Sequence , Chemical Precipitation , Chromatography, Ion Exchange , Enzyme Stability , Glucose/chemistry , Hydrogen-Ion Concentration , Kinetics , Molecular Sequence Data , Plant Proteins , Sequence Homology, Amino Acid , Substrate Specificity , beta-Glucosidase/chemistry
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