Food security is importance for people all the world. Bombay locust (Patanga succincta) is a major agricultural pest in Thailand and most popular for consumption as human food. Arthropods include crustacean (shrimp) and insect which can induce allergic reactions in sensitive humans. The aims of this study is to identified the cross-reactive allergens in P. succincta with sera who allergic to shrimp by IgE-immunoblotting and tandem mass spectrometry (LC-MS/MS) and investigated the effect of thermal processing (fried) on allergenicity of this edible insect. The electrophoresis profiles between raw and fried P. succincta is clearly differentiated. Hexamerin (HEX), enolase and arginine kinase (AK) were identified as raw P. succincta allergens whereas fried P. succincta can identified four proteins as HEX, pyruvate kinase, enolase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as allergen. In this result, thermal processing can alter the allergenicity of food allergens. Index Terms-edible insects, patanga succincta, Bombay locust, food processing, fried, allergen, IgE
In order to determine the primary structure of banana shrimp, Penaeus merguiensis, vitellogenin (Vg), we previously purified vitellin (Vt) from the ovaries of vitellogenic females, and chemically analyzed the N-terminal amino acid sequence of its 78 kDa subunit. In this study, a cDNA from this species encoding Vg was cloned based on the N-terminal amino acid sequence of the major 78 kDa subunit of Vt and conserved sequences of Vg/Vt from other crustacean species. The complete nucleotide sequence of Vg cDNA was achieved by RT-PCR and 5' and 3' rapid amplification of cDNA ends (RACE) approaches. The full-length Vg cDNA consisted of 7,961 nucleotides. The open reading frame of this cDNA encoding a precursor peptide was comprised of 2,586 amino acid residues, with a putative processing site, R-X-K/R-R, recognized by subtilisin-like endoproteases. The deduced amino acid sequence was obtained from the Vg cDNA and its amino acid composition showed a high similarity to that of purified Vt. The deduced primary structure, of P. merguiensis Vg was 91.4% identical to the Vg of Penaeus semisulcatus and was also related to the Vg sequences of six other crustacean species with identities that ranged from 86.9% to 36.6%. In addition, the amino acid sequences corresponding to the signal peptide, N-terminal region and C-terminal region of P. merguiensis Vg were almost identical to the same sequences of the seven other reported crustacean species. Results from RT-PCR analysis showed that Vg mRNA expression was present in both the ovary and hepatopancreas of vitellogenic females but was not detected in other tissues including muscle, heart, and intestine of females or in the hepatopancreas of mature males. These results indicate that the Vg gene may be expressed only by mature P. merguiensis females and that both the ovary and hepatopancreas are possible sites for Vg synthesis in this species of shrimp.
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