A panoramic view and swot analysis of artificial intelligence for achieving the sustainable development goals by 2030: progress and prospects

Applied Intelligence - The17 Sustainable Development Goals (SDGs) established by the United Nations Agenda 2030 constitute a global blueprint agenda and instrument for peace and prosperity...     

Current advances in the non‐chromatographic fractionation and characterization of PEGylated proteins

For more than 30 years, PEGylation has been used to improve the physicochemical properties of several proteins and therapeutic drugs having a major impact in the biopharmaceutical industry. The purification of PEGylated proteins usually involves two basic challenges: (1) the separation of PEG‐proteins from other reaction products; and (2) the sub‐fractionation of PEG‐proteins on the basis of their degree of PEGylation and positional isomerism. Currently, most PEGylated protein purification processes are based on chromatographic techniques, especially size exclusion chromatography (SEC) and ion exchange chromatography (IEX). Nonetheless, other less frequently used strategies based on non‐chromatographic techniques such as ultrafiltration, electrophoresis, capillary electrophoresis, and aqueous two‐phase systems have been developed in order to fractionate and analyze PEGylated derivates. This review presents current advances in some of the most widely used non‐chromatographic strategies for the fractionation and analysis of PEG‐protein conjugates. Copyright © 2010 Society of Chemical Industry     

Oxidation of Polycyclic Aromatic Hydrocarbons using Partially Purified Laccase from Residual Compost of Agaricus bisporus

Laccase partially purified from residual compost of Agaricus bisporus by an aqueous two‐phase system (Lac ATPS) was used in degrading polycyclic aromatic hydrocarbons: fluorene (Flu), phenanthrene (Phe), anthracene (Ant), benzo[a]pyrene (BaP), and benzo[a]anthracene (BaA). The capacity of the enzyme to oxidize polyaromatic compounds was compared to that of the crude laccase extract (CE). After treatment of 72 h, Lac ATPS and CE were not capable of oxidizing Flu and Phe, while Ant, BaP, and BaA were oxidized, resulting in percentages of oxidation of 11.2 ± 1, 26 ± 2, and 11.7 ± 4 % with CE, respectively. When Lac ATPS was used, the following percentages of oxidation were obtained: 11.4 ± 3 % for Ant, 34 ± 0.1 % for BaP, and 13.6 ± 2 % for BaA. The results reported here demonstrate the potential application of Lac ATPS for the oxidation of polycyclic aromatic hydrocarbons.     

The Origin of the High Voltage in DPM12/P3HT Organic Solar Cells

Organic solar cells made using a blend of DPM12 and P3HT are studied. The results show that higher V_oc can be obtained when using DPM12 in comparison to the usual mono‐substituted PCBM electron acceptor. Moreover, better device performances are also registered when the cells are irradiated with sun‐simulated light of 10–50 mW cm^?2 intensity. Electrochemical and time‐resolved spectroscopic measurements are compared for both devices and a 100‐mV shift in the density of states (DOS) is observed for DPM12/P3HT devices with respect to PCBM/P3HT solar cells and slow polaron‐recombination dynamics are found for the DPM12/P3HT devices. These observations can be directly correlated with the observed increase in V_oc, which is in contrast with previous results that correlated the higher V_oc with different ideality factors obtained using dark‐diode measurements. The origin for the shift in the DOS can be correlated to the crystallinity of the blend that is influenced by the properties of the included fullerene.     

New aqueous two‐phase systems based on poly(ethylene oxide sulfide) (PEOS) and potassium phosphate for the potential recovery of proteins

A new aqueous two‐phase system (ATPS) based on a degradable polymer called poly(ethylene oxide sulfide) with a molecular weight of 33 000 g mol^?1 (identified as PEOS‐12) and potassium phosphate was exploited for the potential recovery of proteins. An initial characterisation of the ATPS was achieved by the construction of a phase diagram for the PEOS‐12/phosphate system. The protein partitioning behaviour of lysozyme and bovine serum albumin (BSA), selected as single model proteins, and B‐phycoerythrin (BPE) produced by Porphyridium cruentum in the new ATPS under increasing tie line length (TLL) conditions at constant phase volume ratio (V_r) and system pH was investigated. Both single proteins partitioned in the new ATPS, initially exhibiting bottom phase preference; however, lysozyme changed phase preference when TLL was increased. Fractionation of a complex model (production of BPE by P. cruentum) using PEOS‐12/phosphate ATPS was performed to evaluate the potential protein recovery from fermentation broth or cell homogenate. The proposed new ATPS proved to be suitable for the potential recovery of BPE from crude extract of P. cruentum. In general, a system comprising V_r = 1.0, 18% (w/w) PEOS‐12, 8% (w/w) phosphate and 30% (w/w) TLL at pH 7.0 provided conditions to concentrate BPE into the bottom phase (i.e. partitioning behaviour of BPE; lnK_BPE = ?1.8) with a protein recovery of 84%. The findings reported here demonstrate the potential application of the new ATPS for the recovery of proteins from complex biological suspensions. Copyright © 2006 Society of Chemical Industry