Effects of pH-shifting and ultrasound on the structural and emulsifying properties of peanut globulin fractions.

This work investigated and compared the structural and emulsifying properties of peanut globulin fractions (conarachin and arachin) after ultrasonication (US) and pH2.5-shifting treatments, singly and in combination. Results showed that pH2.5-shifting was more effective in degrading peanut protein subunits and unfolding their structures than US treatment. Conarachin tended to aggregate during US and pH2.5-shifting treatments possibly due to higher free sulfhydryl content, while high molecular weight arachin tended to disaggregate during these treatments. pH2.5-shifting or US+pH2.5-shifting treatments significantly increased the surface hydrophobicity of conarachin (from 72 to 314) and arachin (from 336 to 888), which may be responsible for the enhancement of protein emulsifying activity. All treatments significantly improved the physical stability of arachin-stabilized emulsions with higher absolute potentials but lowered that of conarachin-stabilized emulsions. However, pH2.5-shifting or US+pH2.5-shifting treatments could improve the stability of conarachin-stabilized emulsions in the presence of salts.

Structural and functional properties of self-assembled peanut protein nanoparticles prepared by ultrasonic treatment: Effects of ultrasound intensity and protein concentration.

Peanut protein isolate (PPI) nanoparticles were prepared by self-assembly under the combined action of ultrasound (US) and protein concentration. The effects of ultrasound intensity (150-500 W) and protein concentration (1-12 %, w/v) on the structural and functional properties of PPI nanoparticles were investigated. Low-intensity US significantly increased the particle size of PPI, but high-intensity US decreased it. The largest PPI nanoparticles were obtained when 10 % PPI was subjected to low-intensity US treatment (200 W for 5 min). These nanoparticles possessed unique structural characteristics, such as the lowest absolute ζ-potential and the highest contents of exposed free sulfhydryl and disulfide bond, which may be responsible for their excellent heat-set gelling properties. The 12 % PPI treated with low- and high-intensity US had the highest emulsifying activity index and emulsifying stability index, respectively. The self-assembled PPI nanoparticles induced by US treatments at high protein concentrations have great potentials for application in the food industry.

Coating function and stabilizing effects of surface layer protein from Lactobacillus acidophilus ATCC 4356 on liposomes.

Surface layer proteins (SLPs) are crystalline arrays in the outermost layer of cell envelope in many archaea and bacteria. SLPs subunits have the ability to reassemble on the surface of lipid layers. In this work, the SLP from Lactobacillus acidophilus ATCC 4356 was extracted and reassembled on the surface of positively charged liposomes composed of dipalmitoyl phosphatidylcholine, cholesterol and octadecylamine. Zeta potentials and particle size were determined to describe the adsorption process of SLP on liposomes. The liposomes completely coated with SLP were observed by transmission electron microscope. To investigate the stabilizing effects of SLP on liposomes, carboxyfluorescein (CF) was encapsulated and its leakage was determined as an evaluation index. The results showed that the L. acidophilus ATCC 4356 SLP significantly (P < 0.05) increased the stability of the liposomes in the course of thermal challenge. Furthermore, SLP was able to reduce the aggregation of liposomes in serum. Storage stability of liposomes was performed at 25 °C, 4 °C and -20 °C for 90 days. And the SLP-coated liposomes released less CF than the control liposomes during storage at the three evaluated temperatures. Our findings extended the application field of Lactobacillus SLPs and introduced a novel nanocarrier system with good chemical stability.

[Clinical outcome of tibiotalocalcaneal fusion using cannulated screw and humeral proximal locking plate inverted fixation through a lateral transfibular approach].

OBJECTIVE: To evaluate the clinical outcome of tibiotalocalcaneal fusion using cannulated screw and humeral proximal locking plate inverted fixation through a lateral transfibular approach. METHODS: From June 2015 to December 2018, 15 patients underwent a tibiotalocalcaneal fusion operation using cannulated screw and inverted proximal humerus locking plate through a transfibular approach. There were 10 males and 5 females with the age ranging from 45 to 72 (58.9±6.1) years, and the course of disease ranged from 2 to 35 (11.9±7.9)years. Preoperative diagnosis included 8 cases of post traumatic arthritis, 2 cases of Charcot arthritis, 2 cases of Charcot-Marie -Tooth (CMT), 1 case of ankle tuberculosis, 1 case of talar necrosis, and 1 case of pigmented villonnodular synovitis. Among them, 8 patients were combined with simple varus deformity, 4 patients with simple valgus deformity, 2 patients with equinovarus deformity, 1 patient with equinovarus deformity, 2 patients with adduction and internal rotation of middle and forefoot. American Orthopaedic Foot and Ankle Society (AOFAS) ankle and hindfoot score and the visual analogue scale (VAS) score were used to evaluate the clinical outcome at the last follow up. RESULTS: One lost follow up and remaining fourteen patients were followed up. The follow up time ranged from 10 to 25(16.6±4.3) months. All the 15 patients had primary healing. Fusion time ranged from 15 to 24 (16.8 ± 2.4) weeks after operation. One patient with diabetes experienced delayed union and was successfully treated with secondary bone grafting combined with Platelet-Rich Plasma (PRP) injection. The AOFAS score increased from 38.7±3.3 to 84.5±2.6 (P<0.05), and the VAS score decreased from 7.5±1.6 to 1.9±0.3(P<0.05). CONCLUSION: Tibiotalocalcaneal fusion used cannulated screw and humeral proximal locking plate inverted fixation through a lateral transfibular approach has the advantages of relatively simple technique, high fusion rate, especially for patients with posterior foot deformity, which has satisfactory short term effects.

Feasibility analysis of external application of Xiao-Shuan-San in preventing PICC-related thrombosis.

PURPOSE: We aim to analyze the feasibility of external application of Xiao-Shuan-Santo prevent peripherally inserted central catheter (PICC) -related thrombosis. METHODS: A total of 218 patients with PICC catheterization were randomly divided into a control group (n = 103) and a treatment group (n = 115). Patients in the treatment group received additional external application of Xiao-Shuan-San. The changes of coagulation index, the incidence of PICC-related thrombosis and other complications, and the maximum blood flow rate (Vmax) of axillary vein were observed at 1 day before catheterization and 30 days after PICC. RESULTS: At 30 days after PICC, the incidence of PICC-related thrombosis and other adverse events in the treatment group were obviously lower than that in the control group (P < 0.05), and the decreased Vmax value of axillary vein in the control group (11.75±1.91 cm/s) was more visible than that in the treatment group (14.63±3.03 cm/s), accompanied by a statistical significance (P < 0.05). CONCLUSIONS: External application of Xiao-Shuan-San could reduce the incidence of PICC-related thrombosis and other complications.

In vitro antithrombotic activities of peanut protein hydrolysates.

The antithrombotic activities of peanut protein hydrolysates were investigated using a microplates assay. When peanut proteins were hydrolyzed to a limited extent by various enzymes, their thrombin inhibitory abilities were significantly enhanced. However, the resultant hydrolysates showed significantly different activities even at the same degrees of hydrolysis. The hydrolysates generated by Alcalase 2.4L displayed the best antithrombotic activities and the hydrolysis process was further optimized by response surface methodology. The antithrombotic activities were increased to 86% based on a protein concentration of 50mg/ml under the optimal conditions: pH 8.5, enzyme concentration of 5000IU/g of peanut proteins, and 2h hydrolysis time at 50°C. The Alcalase 2.4L crude hydrolysates were then fractionated successively by preparative and semi-preparative reverse-phase high-performance liquid chromatography (RP-HPLC). The peptide fraction collected inhibited thrombin-catalyzed coagulation of fibrinogen completely at a concentration of 0.4mg/ml, with an antithrombotic activity close to that of heparin at quite a low concentration (0.2mg/ml). This peptide fraction was further analyzed by online reverse-phase ultra-performance liquid chromatography (RP-UPLC) coupled to matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS), and three new peptides were identified as Ser-Trp-Ala-Gln-Leu, Gly-Asn-His-Glu-Ala-Gly-Glu and Cys-Phe-Asn-Glu-Tyr-Glu, respectively. This research provided an effective way to produce antithrombotic peptides from peanut proteins, and also helped to elucidate the structure-function relationships of peanut peptides.