Dietary fibres from cassava residue: Physicochemical and enzymatic improvement, structure and physical properties

In this study, an physico-chemical method and enzymatic improvement were used to extract cassava dietary fiber from cassava residue. α-amylase, glucoamylase, lipase, and protease were added to the physically comminuted cassava residue to remove starch, fat, and protein. Then, with the aid of ultrasound, dietary fiber was bleached with hydrogen peroxide to increase its whiteness. Finally, the cassava dietary fiber was treated with cellulase to increase the amount of soluble dietary fiber. The yield of dietary fiber was 75.63%, 37.55% of which was soluble dietary fiber. Water-holding capacity, water-swelling capacity, and oil-holding capacity of cassava dietary fiber were 4.020 g/g, 2.091 mL/g, and 2.891 g/g, respectively, which were 11.14%, 52.85%, and 9.55% higher than those of raw tapioca. Thus, the physical and chemical properties of the dietary fiber were improved

Tunable Interlayer Shifting in Two-Dimensional Covalent Organic Frameworks Triggered by CO2 Sorption

10.1021/jacs.2c08214Journal of the American Chemical Society1444420363–2037

High-Throughput and Rapid Screening of Novel ACE Inhibitory Peptides from Sericin Source and Inhibition Mechanism by Using in Silico and in Vitro Prescriptions

Several novel peptides with high ACE-I inhibitory activity were successfully screened from sericin hydrolysate (SH) by coupling in silico and in vitro approaches for the first time. Most screening processes for ACE-I inhibitory peptides were achieved through high-throughput in silico simulation followed by in vitro verification. QSAR model based predicted results indicated that the ACE-I inhibitory activity of these SH peptides and six chosen peptides exhibited moderate high ACE-I inhibitory activities (log IC₅₀ values: 1.63–2.34). Moreover, two tripeptides among the chosen six peptides were selected for ACE-I inhibition mechanism analysis which based on Lineweaver–Burk plots indicated that they behave as competitive ACE-I inhibitors. The C-terminal residues of short-chain peptides that contain more H-bond acceptor groups could easily form hydrogen bonds with ACE-I and have higher ACE-I inhibitory activity. Overall, sericin protein as a strong ACE-I inhibition source could be deemed a promising agent for antihypertension applications

Temperature-dependent rearrangement of gas molecules in ultramicroporous materials for tunable adsorption of CO2 and C2H2

Abstract The interactions between adsorbed gas molecules within porous metal-organic frameworks are crucial to gas selectivity but remain poorly explored. Here, we report the modulation of packing geometries of CO2 and C2H2 clusters within the ultramicroporous CUK-1 material as a function of temperature. In-situ synchrotron X-ray diffraction reveals a unique temperature-dependent reversal of CO2 and C2H2 adsorption affinities on CUK-1, which is validated by gas sorption and dynamic breakthrough experiments, affording high-purity C2H2 (99.95%) from the equimolar mixture of C2H2/CO2 via a one-step purification process. At low temperatures (10) and capacity (170 cm3 g−1) owing to the formation of CO2 tetramers that simultaneously maximize the guest-guest and host-guest interactions. At room temperature, conventionally selective adsorption of C2H2 is observed. The selectivity reversal, structural robustness, and facile regeneration of CUK-1 suggest its potential for producing high-purity C2H2 by temperature-swing sorption