Abstract

Water-soluble proteins extracted from two species of grasshoppers,Patanga succincta(WSPP) andChondracris roseapbrunner(WSPC), were characterized as well as their functional properties and antioxidant activities were investigated. The extraction yield, on a wet weight basis, was 7.35% and 7.46% for WSPP and WSPC,respectively. The most abundant amino acid in both proteins was glutamic acid, followed by aspartic, alanine, and leucine, in that order. The electrophoretic study revealed that proteins with MW of 29, 42, 50, 69, and 146 kDa were the major protein components in WSPP and WSPC. FTIR analysis showed that those proteins remained their structural integrity. The surface hydrophobicity at pH 7 of WSPC was higher than WSPP, but the sulfhydryl group content did not show significant difference between the proteins from two species. Both grasshopper proteins were mostly soluble in strong acidic and alkaline aqueous solutions with a minimum value at pH 4. Those proteins exhibited poor emulsifying properties and foaming capacity, but they had greater foaming stability compared with bovine serum albumin (BSA) (p<0.05). WSPC showed greater DPPH•and ABTS•+scavenging activities and ferric-reducing antioxidant power (FRAP) than did WSPP (p<0.05). Therefore, based on characteristics and functional properties, water-soluble proteins from both edible grasshoppers can be used as an ingredient in food applications.

Highlights

  • In 2050, the world population is estimated at more than 9 billion people, resulting in an additional need for food and feed outputs [1]

  • Extraction efficiency was calculated as a percentage of the total protein extracted from P. succincta and C. roseapbrunner for WSPP and WSPC, respectively, in comparison with that of its protein content, which was determined by the Kjeldahl method [16]. e extraction efficiency of each WSPP and WSPC was calculated as follows: extraction efficiency(%)

  • One gram of WSPP and WSPC was mixed with 9 mL of distilled water and stirred at 100 rpm for 10 min. e pH value of the mixture was measured at room temperature in triplicate using an electronic pH meter (FE20, Mettler-Toledo Instruments Co., Ltd., Switzerland)

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Summary

Introduction

In 2050, the world population is estimated at more than 9 billion people, resulting in an additional need for food and feed outputs [1]. In countryside of Northern and Northeastern ailand, people consume several species of insects including grasshoppers, crickets, beetles, silkworm pupae, and bamboo worm. Edible insects have higher crude protein content and have been reported to be a good source of essential amino acids [4]. Yi et al [8] reported poor foam and gelling properties of five different acid-extracted insect proteins, including those from a cricket (Acheta domesticus). E aim of this investigation was, to characterize and compare the functional properties as well as antioxidant activities of water-soluble proteins from two species of grasshoppers (P. succincta and C. roseapbrunner), commonly found in ailand, for their potential use as an alternative source of protein in food ingredients Yang et al [14] reported polyunsaturated fatty acid content of 6 species of edible insects from ailand to range from 726 to 2883 mg/100 g and monounsaturated fatty acid content to range from 714 to 5889 mg/100 g. is leads to the fact that edible insects are a potential source of fat and protein, but there is limited information on the characteristics and functional properties of extracted edible protein from specific insects. e aim of this investigation was, to characterize and compare the functional properties as well as antioxidant activities of water-soluble proteins from two species of grasshoppers (P. succincta and C. roseapbrunner), commonly found in ailand, for their potential use as an alternative source of protein in food ingredients

Materials and Methods
Physicochemical Characterization
Evaluation of Functional Properties
Determination of Antioxidant Activities
Results and Discussion
Physicochemical Characteristics of Grasshopper Proteins
Functional Properties
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