Qingli Yang

Extraction and Characterization of Chitin from the Beetle Holotrichia parallela Motschulsky

Insect chitin was isolated from adult Holotrichia parallela by treatment with 1 M HCl and 1 M NaOH, following by 1% potassium permanganate solution for decolorization. The yield of chitin from this species is 15%. This insect chitin was compared with the commercial α-chitin from shrimp, by infrared spectroscopy, X-ray diffraction, scanning electron microscopy, and elemental analysis. Both chitins exhibited similar chemical structures and physicochemical properties. Adult H. parallela is thus a promising alternative source of chitin.

Chemical composition and antioxidant activities of Broussonetia papyrifera fruits.

Fruits of Broussonetia papyrifera from South China were analyzed for their total chemical composition, and antioxidant activities in ethanol and aqueous extracts. In the fruit of this plant, the crude protein, crude fat and carbohydrates was 7.08%, 3.72% and 64.73% of dry weight, respectively. The crude protein, crude fat and carbohydrates were 15.71%, 20.51% and 36.09% of dry weight, respectively. Fatty acid and amino acid composition of the fruit were analyzed. Unsaturated fatty acid concentration was 70.6% of the total fatty acids. The percentage of the essential amino acids (EAAs) was 40.60% of the total amino acids. Furthermore, B. papyrifera fruit are rich in many mineral elements and vitamins. Total phenolic content was assessed using the Folin-Ciocalteau assay, whereas antioxidant activities were assessed by measuring the ability of the two extracts to scavenge DPPH radicals, inhibit peroxidation, and chelate ferric ions. Their reducing power was also assessed. Results indicated that the aqueous extract of B. papyrifera was a more potent reducing agent and radical-scavenger than the ethanol extract. GC–MS analysis of the ethanol extract showed the presence of some acid-containing compounds. The changes in total phenolic content and antioxidant capacity in B. papyrifera from four different regions grown under normal conditions were assessed. The antioxidant activity of different extracts was positively associated with their total phenolic content. These results suggest that the fruit of B. papyrifera could be used in dietary supplement preparations, or as a food additive, for nutritional gain, or to prevent oxidation in food products.

Ultrasonic-Assisted Enzymolysis to Improve the Antioxidant Activities of Peanut (Arachin conarachin L.) Antioxidant Hydrolysate

The objective of this work is to provide a theoretical basis for preparing peanut antioxidant hydrolysate in order to improve its antioxidant activities. Therefore, response surface methodology (RSM) based on the Box-Behnken design was used to optimize ultrasonic-assisted enzymolysis for the purpose of preparing peanut antioxidant hydrolysate. Results indicated that the DPPH free radical scavenging activity of peanut hydrolysate could reach 90.06% under the following optimum conditions: ultrasonic power of 150.0 w, reaction temperature of 62.0 °C, incubation time of 25.0 min, and initial pH value of 8.5. The DPPH free radical scavenging rate of peanut hydrolysate from ultrasonic-assisted enzymolysis improved comparing with that of peanut hydrolysate from protease hydrolysis alone. The peanut antioxidant hydrolysate was found to display eight improved kinds of antioxidant activities. In conclusion, the optimal ultrasonic-assisted enzymolysis technology conditions described in this paper, appear to be beneficial for preparing peanut antioxidant hydrolysate.

Antioxidant activity and phenolic compounds of Holotrichia parallela Motschulsky extracts.

Insects have been relatively unexplored as potential sources of natural antioxidants. We report the antioxidant activity of extracts of the adult large black chafer beetle Holotrichia parallela Motschulsky, a common crop pest in China. The antioxidant activity of the ethanolic extract (EE) and the water extract (WE) of adult H. parallela were evaluated by four different in vitro assays. EE showed potent metal-chelating activity and inhibition of lipid peroxidation. WE proved to be an excellent antioxidant in the scavenging of 2,2-diphenyl-1-picrylhydrazyl (DPPH) radicals and metal-chelating activity. Catechin was identified in the ethanolic extract and proteins were the main components in the water extracts. Both compounds could contribute to the antioxidant activity of the species. These results suggest that adult H. parallela might be used as a nutraceutical to alleviate oxidate-induced diseases and as a natural antioxidant additive in the food industry.

Preparation, characterisation and physicochemical properties of the phosphate modified peanut protein obtained from Arachin Conarachin L.

The objective of this work is to obtain a new phosphate modified peanut protein (PMPP) with good physicochemical properties by using a simple and reliable method. For this purpose, response surface methodology (RSM), based on a Box-Behnken design, was used to optimise conditions for the microwave-assisted formation of phosphate modified peanut protein isolate (PPI) with sodium tripolyphosphate (STP) as the substrate. The results indicate that emulsification activity index (EAI) was optimised at 65.04 m(2)/g under the following conditions: substrate mass fraction of 10%, initial pH of 9.90, STP mass fraction of 7.70%, microwave power of 800 W, reaction temperature of 43.0 °C, and incubation time of 3.15 min. The emulsification activity of PPI improved after phosphate modification. Phosphatisation of both the Ser and Thr hydroxyl groups and the Lys amino groups was confirmed for the reaction between STP and PPI according to analysis of FTIR, XRD, TG/DTA, NMR-(31)P and SEM of the product. Physicochemical properties of PMPP were better than those of PPI.

Nutritional Composition and Protein Quality of the Edible Beetle Holotrichia parallela

ABSTRACT. The adult edible beetle Holotrichia parallela Motschulsky (Coleoptera: Scarabaeoidea) represents a traditional food source in China. Based on nutritional analyses, adult H. parallela is high in protein (70%) and minerals and low in fat. H. parallela contained approximately 10% chitin; the corrected protein content was 66%. Oleic acid and linoleic acid were the most abundant fatty acids. Of the total amino acids in H. parallela, 47.4% were essential amino acids. The amino acid scores were 87 and 100, based on the corrected crude and net protein contents, respectively; threonine was the limiting amino acid. In vitro protein digestibility was 78%, and the protein digestibility-corrected amino acid score was 89 based on the net protein content. Adult H. parallela may be a potential source of proteins and minerals for humans and animals.

Optimization of a Microwave-Coupled Enzymatic Digestion Process to Prepare Peanut Peptides

The best enzyme to prepare peanut peptides, papain, coupled with microwave irradiation was selected from five common proteases according to the results of the yield of peanut peptides [nitrogen solution index (NSI) in trichloroacetic acid (TCA), TCA-NSI] and the degree of hydrolysis (DH). The main factors that influenced the microwave-coupled enzymatic digestion method were optimized by response surface analysis. The optimal conditions obtained were as follows: microwave extraction time, 9.5 min; power, 600 W; substrate concentration, 4%; enzymatic reaction temperature, 50 °C; enzyme quantity, 6,500 U/g; pH, 7.1 (phosphate buffer, 0.05 mol/L). Under these conditions, TCA-NSI was 62.00% and DH was 25.89%, which is higher than that obtained with either protease hydrolysis or microwave hydrolysis alone.

Purification and Identification of a Natural Lectin from the Seed of Peanut Arachis hypogaea

A natural lectin from the seed of peanut Arachis hypogaea was purified by singlestep affinity chromatography using galactoside-coupled agarose. The native molecular mass of purified A. hypogaea lectin (PN-L) was 29 kDa. The lectin PN-L was detected for agglutinating activity, glycoinhibiting action and thermostability. The influence of pH on those activities was also tested. The results showed that PN-L could not agglutinate three kinds of human erythrocytes. But it showed a strong affinity to human A, B and O erythrocytes (RBC) treated by neuraminidase. Agglutinating activity of PN-L to neuraminidase treated human O erythrocytes was inhibited by lactose, raffinose, melibiose and D-galactose. The agglutinating activity of peanut seed lectin was stable up to 55°C and at pH 5.0-11.0. The results of MALDI-TOF- TOF analysis indicated that the protein PN-L showed highly homology with the Peanut Lectin Chain A protein (gi|1942899).