Correlation between in vitro starch digestibility and starch structure/physicochemical properties in rice.

Natural resistant starch (RS) in rice provides human health benefits, and its concentration in rice is influenced by the structure and physicochemical properties of starch. The native starch structures and physicochemical properties of three rice varieties, QR, BR58, and BR50, and their relationships to in vitro digestibility were studied. The starch granules in all three varieties were irregular or polyhedral in shape. There were a few oval granules and a few pinhole structures in QR, no oval granules but a higher number of pinholes in BR58, and no oval granules and pinholes in BR50. QR is a low-amylose (13.8 %), low-RS (0.2 %) variety. BR58 is a low-amylose (15.3 %), high-RS (6.5 %) variety. BR50 is a high-amylose (26.7 %), high-RS (8.3 %) variety. All three starches exhibited typical A-type diffraction patterns. Starch molecular weight, chain length distribution, starch branching degree, pasting capabilities, and thermal properties differed considerably between the rice starches. The RS contents of the rice starch varieties were positively correlated with AAC, Mw/Mn, Mz/Mn, peak 3, B, PTime, and Tp and negatively correlated with Mn, peak 2, DB, PV, and BD, according to Pearson's correlation analysis. These findings may be helpful for the breeding and development of high-RS rice varieties.

An Organic Redox Mediator with a Defense-Donor for Lithium Anode in Lithium-Oxygen Batteries.

Lithium-oxygen batteries (LOBs) suffer from large charge overpotential and unstable Li metal interface, which can be attributed to the inefficient charge transport at the insulating Li2 O2 /cathode interface and the severe oxygen corrosion issue on the Li anode surface. The use of soluble redox mediators (RMs) can effectively enhance the charge transport between Li2 O2 and cathode, thus greatly reducing the charge overpotential. However, oxidized RMs will also shuttle to the anode side and react with the Li metal, which not only results in the loss of both the RMs and the electrical energy efficiency but also exacerbates the Li anode corrosion. Herein, an organic compound-acetylthiocholine iodide (ATCI), in which a big cation group is contained, is proposed as a defense-donor RM for lithium anode in LOBs to simultaneously address the above issues. During charge, it can accelerate the oxidation kinetics of Li2 O2 via its iodide anion redox couple (I- /I3 - ). Meanwhile, its cation segment (ATC+ ) can move to the anode surface via electric attraction and in situ forms a protective interfacial layer, which prevents the Li anode from the attack of oxidized RM and oxygen species. Consequently, the ATCI-containing LOBs can achieve both a low charge potential (≈3.49 V) and a long cycle life (≈190 cycles).

High-Performance Lithium-Oxygen Batteries Using a Urea-Based Electrolyte with Kinetically Favorable One-Electron Li2 O2 Oxidation Pathways.

Glymes are the most widely used electrolyte solvents in lithium-oxygen batteries (LOBs) due to their relatively high stability. However, their associated LOBs have long been plagued by large charge overpotential, which is closely related to the sluggish two-electron Li2 O2 oxidation mechanism. Here, we report a new electrolyte solvent-1,1,3,3-tetramethylurea (TMU) for LOBs with high performance and an alternative mechanism, where a kinetically favorable one-electron Li2 O2 oxidation pathway can happen in the urea electrolyte system, thus leading to a much lower charge overpotential (≈0.51 V) compared to the tetraglyme-based LOBs (≈1.27 V). Besides, TMU also exhibits good stability since it does not contain any α-hydrogen atoms that are vulnerable to be attacked by superoxide species, thus suppressing the hydrogen abstraction side reactions. Consequently, the TMU-based LOBs can stably work for more than 135 cycles, which is four times that of the tetraglyme-based LOBs (≈28 cycles).

Isolation of two Locust protein targets of a protein tyrosine phosphatase from Metarhizium anisopliae strain CQMa102.

In entomopathogenic fungi, secretory protein phosphatases might function in the utilization of phosphoproteins from the environment. But if secreted into the host, secretory protein phosphatases might play a role in pathogenesis by dephosphorylation of host phosphoproteins. Our group purified a novel phosphatase from entomopathogenic fungi, Metarhizium anisopliae. The substrate specificity and inhibitor sensitivity indicate that the phosphatase is a protein tyrosine phosphatase (PTPase). In order to analyze the targets of the PTPase in Locusta migratoria hemolymph, two-dimensional electrophoresis and mass spectrometry were used. The results indicated that the PTPase could specifically dephosphorylate two phosphoproteins from L. migratoria hemolymph. One phosphoprotein was identified as trans-Golgi p230. Previous studies have shown that trans-Golgi p230 participates in vesicular transport of functional proteins from the distal Golgi compartment. trans-Golgi p230 can be inactivated by dephosphorylation, which implies that M. anisopliae could interfere with the correct transportation of functional proteins by secreting extracellular PTPase into the hemolymph. There are some secretion proteins, such as transferrin, have been thought to participate in the insect innate immune against microbial infection, therefor M. anisopliae could interfere with immune defenses of L. migratoria by secreting extracellular PTPase into the hemolymph.

Differentially-expressed glycoproteins in Locusta migratoria hemolymph infected with Metarhizium anisopliae.

Glycoproteins play important roles in insect physiology. Infection with pathogen always results in the differential expression of some glycoproteins, which may be involved in host-pathogen interactions. In this report, differentially-expressed glycoproteins from the hemolymph of locusts infected with Metarhizium anisopliae were analyzed by two-dimensional electrophoresis (2-DE) and PDQuest software. The results showed that 13 spots were differentially expressed, of which nine spots were upregulated and four were downregulated. Using MS/MS with de novo sequencing and NCBI database searches, three upregulated proteins were identified as locust transferrin, apolipoprotein precursor, and hexameric storage protein 3. These proteins have been reported to be involved in the insect innate immune response to microbial challenge. Due to the limited available genome information and protein sequences of locusts, the possible functions of the other 10 differentially-expressed spots remain unknown.