No abstract

Boiling and frying can alter the structure of peanut allergens and therefore change the IgE‐binding capacity of the Ara h 1. In this research, we aim to clarify the connections between structural changes and the allergenicity alteration, and recommend an effective thermal method to minimize the allergenicity of Ara h 1. Anion exchange chromatography was used to isolate Ara h 1 from non/heat‐treated peanuts. Ara h 1 in boiled peanuts has a relatively low hydrophobic index, reduced maximum emission wavelength in the fluorescence, less content of α‐helix, and the lowest IgE‐binding efficiency. On the contrary, Ara h 1 in fried peanuts present a much higher degeneration degree, a red shift in fluorescence, and a decrease in the content of α‐helix. These data indicate that boiling can reduce the allergenicity of Ara h 1, thus can be utilized in peanut processing from a security point of view.

Food processing affects the bioavailability and immunoreactivity of allergens. However, there was a lack of the combined study of the influence of the processing and gastrointestinal digestion on peanut matrix. Digestibility of peanut matrices was assessed by using an in vitro digestion model and monitored by SDS-PAGE, immunoblotting with polyclonal antibody and serum from peanut-allergic patients. The IgE-binding ability of digested samples will be assessed by immunoassay. Peanut proteins were digested by pepsin after only 2 min which was accompanied by a loss of high molecular weight proteins and enrichment in polypeptides with molecular weight lower than 10 kDa. Ara h 1 and Ara h 3 were partly proteolysis, and Ara h 2/6 containing a digestion-resistant fragment. All soluble fractions after 120 min gastric digestion reduced a higher IgE-binding ability than that after 10 min. Our findings provide a more realistic picture, considering the role of food processing and food matrix. ARTICLE HISTORY

of main observation and conclusion Molecular geometry engineering is an effective strategy to control the micromorphology and molecular energy level in organic photovoltaics (OPVs). Two novel copolymers based on alkylsilyl-and chloride-functionalized benzodithiophene (BDT) were designed and synthesized for wide bandgap copolymer donor materials in OPVs. It was found that the two copolymers exhibited distinctly different properties in active layer when blended with fullerene-free acceptor IT-4F. The chloride-functionalized copolymer PBDTCl-TZ with deeper molecular energy level and better coplanar structure induced more ordered aggregation in blend film. Thus, the device based on PBDTCl-TZ exhibits better energy alignment with IT-4F and smaller radiative recombination. Furthermore, the non-radiative recombination of PBDTCl-TZ:IT-4F based device is about 45 mV lower than the PBDTSi-TZ:IT-4F based device, contributing to a lower energy loss (E loss), and a higher open-circut voltage (V OC). As a result, the devices based on the blend of PBDTCl-TZ:IT-4F exhibit a high power conversion efficiency (PCE) of up to 12.2% with a high V OC of 0.837 V, higher than that of PBDTSi-TZ:IT-4F, of which the PCE is 11.2% with a V OC of 0.781 V.

Ara h 1 is a key peanut allergen and its activity is significantly affected by protein intrinsic structure which is found to be regulated by heat treatment, although the molecular basis for this regulation has remained largely unknown. Here, we explored the effect of boiling on the structure and allergenicity of recombinant peanut protein Ara h 1 (rAra h 1). rAra h 1 was purified from E. Coli BL21(DE3) plysS cells and structurally studied. According to the results, rAra h 1 undergoes degradation during the heating process, and the aggregation of fragments happened after 20 min of heating. An increased surface hydrophobic index and a decreased content of α-helixes were found in rAra h 1, indicating a looser protein structure of rAra h 1 caused by heat treatment. Destroyed epitopes during protein degradation and aggregation could be a mechanism of reducing the allergenic nature of rAra h 1 by heat treatment. ARTICLE HISTORY