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1.
Biophys Rev ; 13(6): 925-930, 2021 Dec.
Article in English | MEDLINE | ID: mdl-35059018

ABSTRACT

This review is directed to researchers interested in a new point of view with relevance to nano-biomedicine. The first part covers the uses and potential of diacetylene lipid, 1,2-bis(10,12-tricosadiynoyl)-sn-glycero-3-phosphocholine (DC8,9PC) in facilitating biological target recognition. The second part concentrates on the use of albumin as a "soft" coating for nanoparticles. This review makes comment on how fabricated nanoparticles will assist with future human health applications.

2.
Biotechnol Lett ; 26(16): 1265-8, 2004 Aug.
Article in English | MEDLINE | ID: mdl-15483384

ABSTRACT

Affinity chromatography with immobilised triazine dyes was used to separate the main enzymes present in the naringinase complex produced by Aspergillus terreus CECT 2663. One alpha-L-rhamnosidase and two beta-D-glucosidases (beta G1 and beta G2) were separated by a simple two-step procedure involving chromatography with Red HE-3B immobilised on Sepharose 4B first at pH 5.5 and then at pH 4.7. Maximum activity of the beta-D-glucosidases was from pH 4 to 6 and at 65 degrees C. Both glucosidases were active on p -nitrophenol glucoside and prunin with respective Km values of 1.9 mm and 1.6 mm for beta G1 and 2.1 mm and 0.25 mm for beta G2. Only beta G1 hydrolysed cellobiose (Km = 5.7 mm).


Subject(s)
Aspergillus/enzymology , Chemical Fractionation/methods , Chromatography, Affinity/methods , Chromatography, Agarose/methods , Glycoside Hydrolases/biosynthesis , Glycoside Hydrolases/isolation & purification , Multienzyme Complexes/biosynthesis , Multienzyme Complexes/isolation & purification , Triazines , beta-Glucosidase/biosynthesis , beta-Glucosidase/isolation & purification , Adsorption , Coloring Agents , Enzyme Activation , Glycoside Hydrolases/chemistry , Hydrogen-Ion Concentration , Multienzyme Complexes/chemistry , Temperature , beta-Glucosidase/chemistry
3.
Bioseparation ; 9(3): 173-7, 2000.
Article in English | MEDLINE | ID: mdl-11105247

ABSTRACT

Immobilised metal ion affinity polysulfone hollow-fibre membranes, with a high capacity for protein adsorption, were prepared and their utilisation for commercial pectic enzyme fractionation was studied. The pass-through fraction containing pectinlyase is useful for fruit-juice clarification without methanol production on account of pectinesterase being retained by the IDA-Cu2+ membrane.


Subject(s)
Chromatography, Affinity/methods , Polygalacturonase/isolation & purification , Polysaccharide-Lyases/isolation & purification , Copper , Imino Acids
4.
Biotechnol Prog ; 15(3): 500-5, 1999 May.
Article in English | MEDLINE | ID: mdl-10356269

ABSTRACT

A sulfonic group (up to 200 &mgr;mol/mL) membrane was incorporated to epoxy-activated microporous hollow fibers to obtain high-capacity convective ion exchangers. The pure water flux through the membrane decreased exponentially with sulfonic group density and protein binding capacity increased accordingly. At sulfonic group density of 70 &mgr;mol/mL, the membrane lysozyme maximum binding capacity was 84 +/- 9 mg/mL in comparison with its theoretical monolayer maximum binding capacity of 20 mg/mL, thus evidencing tentacle formation. After a cycle of adsorption in a 30 mM sodium phosphate buffer, pH 7. 0, adsorbed lysozyme could be quantitatively recovered following elution with 0.5 M NaCl in the same buffer. Dynamic capacity for lysozyme was 67% of maximum binding, and this value did not change at space velocities ranging from 10 to 40 min-1 as shown by the superimposition of the corresponding breakthrough curves. A cartridge assembled with 21 fibers showed a dynamic-to-static capacity ratio for lysozyme of 0.60 with 1 mg/mL pure lysozyme solution, and 0.42 with a particulate feed composed of 1 mg/mL lysozyme and 0.1 mg/mL yeast.

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