Gastrointestinal digestibility of micellar casein dispersions: Effects of caprine vs bovine origin, and partial colloidal calcium depletion using in vitro digestion models for the adults and elderly.

In vitro coagulation and digestion of caprine and bovine micellar casein concentrate (MCC) with or without partial colloidal calcium depletion (deCa) were studied under simulated adult and elderly conditions. Gastric clots were smaller and looser for caprine than bovine MCC, and were further looser with deCa and under elderly condition for both caprine and bovine MCC. Casein hydrolysis and concomitant formation of large peptides was faster for caprine than bovine MCC, and with deCa and under adult condition for caprine and bovine MCC. Formation of free amino groups and small peptides were faster for caprine MCC, and with deCa and under adult condition. Upon intestinal digestion, proteolysis occurred rapidly, and was faster under adult condition, but showed less differences with increasing digestion between caprine and bovine MCC, and with and without deCa. These results suggested weakened coagulation and greater digestibility for caprine MCC and MCC with deCa under both conditions.

One-step fabrication of novel MIL-53(Fe, Al) for synergistic adsorption-photocatalytic degradation of tetracycline.

Bimetallic MOFs (MIL-53 (Fe, Al)) were successfully fabricated via a facile one-step solvothermal method for the removal of tetracycline (TC) from aqueous solutions. Tetracycline adsorption and photocatalytic experiments indicate that the optimum bimetallic synthetic molar ratio is 3:2 (40%MIL-53(Fe, Al)). The adsorption data are well fitted by the Freundlich model and pseudo-second-order adsorption kinetics. 40%MIL-53(Fe, Al) has an adsorption capacity of up to 402.033 mg/g. After the dark adsorption phase, 10 mg of 40%MIL-53(Fe, Al) can remove 94.33% of the tetracycline in a 70 mL aqueous solution (20 mg/L) under 50 min irradiation, while only 71.39% and 81.82% of the tetracycline are removed by MIL-53(Fe) and MIL-53(Al) under the same conditions. In addition, 40%MIL-53(Fe, Al) exhibits a significant adsorption-photocatalytic synergy (under direct irradiation without a dark adsorption phase), in which the pseudo-first-order kinetic constant increases by a factor of 3.11. Quenching experiments and ESR characterization indicate that ·O2-, ·OH, and h+ are the main active species in the photocatalytic process. Meanwhile, 40%MIL-53(Fe, Al) demonstrates good stability, with a tetracycline removal rate that still reaches 83.70% after 4 cycles. These results suggest that the prepared 40%MIL-53(Fe, Al) catalyst is a novel adsorption-photocatalytic material that can be used for the efficient treatment of tetracycline.

Novel affinity purification of monomeric sarcosine oxidase expressed in Escherichia coli.

An efficient affinity-purification protocol for Bacillus monomeric sarcosine oxidase (SOX) expressed in Escherichia coli BL21 (DE3) was developed. 4-Aminopyrrole-2-carboxylic acid was chosen as the affinity ligand, which was coupled with Sepharose CL 4B via spacers composed of epichlorohydrin and ethylenediamine. With the affinity medium, the purification process consisted of only one affinity chromatography step to capture monomeric SOX. The purified SOX was 94 and 96% pure when analyzed on an HPLC Vydac C8 column and reducing SDS-PAGE. Meanwhile, the recoveries of typical SOX activity and protein were 90.8 and 37.5%, respectively, which were higher than other reported traditional protocols. Reducing SDS-PAGE analysis revealed that the enzyme was a single polypeptide with the mass of ~46 kDa. The desorption constant Kd and theoretical maximum absorption Qmax were 35 µg/mL and 52.7 mg/g, respectively, in absorption analysis. All results indicated that the method would be of great potential for purifying monomeric SOX on an industrial scale.