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Ionic liquid extraction of silkworm pupa protein and its biological characteristics
Zeng Qing-Lei,Zhang Ning,Zhang Yue-Yue,Xin Xiang-Dong,Attaribo Thomas,Shao Ying,Tang Liu-Mei,Zhang Ran,이광식,진병래,Gui Zhongzheng 한국응용곤충학회 2021 Journal of Asia-Pacific Entomology Vol.24 No.1
Silkworm (Bombyx mori) pupa protein (SPP) is a high-quality source of animal protein with substantial nutri tional benefits and health value. To develop an efficient extraction method for SPP that is environmentally friendly, we selected choline hydroxide ionic liquid (CH-IL) as the extraction solvent and performed orthogonal experiments to optimize the extraction conditions. We demonstrated that 3% CH-IL, a solid-to-liquid ratio (g/mL) of 1:30, an extraction temperature of 40 ◦ C, and an extraction time of 1 h facilitated the most efficient extraction. Compared to the conventional alkali solubilization–acid precipitation method, the CH-IL extraction increased protein content by 12.14%. Protein structure analysis showed that the β-sheet content increased by 10.98% and that of disulfide bonds reduced by 16.4%. The processing properties of the CH-IL extracted protein showed that the solubility, emulsification, and foaming capacity were enhanced by 82.87%, 15.44%, and 18.97%, respec tively. The physical properties of SPP remarkably improved relative to the increased stretching of the poly peptide chains. The findings of this study provide technical knowledge that will enhance the processing performance of pupal proteins.
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Zhiyong Li,Shan Zhao,Xiang-Dong XIN,Bei Zhang,Attaribo Thomas,Asakiya Charles,Kwang Sik Lee,진병래,Zhong-Zheng Gui 한국응용곤충학회 2019 Journal of Asia-Pacific Entomology Vol.22 No.3
Silkworm (Bombyx mori) pupa protein is one potential source of insect protein for use in food. Immunomodulatory peptides are specific protein fragments that can positively influence human health. Here, we purified a novel immunomodulatory hexapeptide from the alcalase hydrolysate of ultramicro-pretreated silkworm pupa proteinusing Sephadex gel filtration chromatography and reverse-phase high-performance liquid chromatography (RP-HPLC). The peptide sequence was determined by liquid chromatography–electrospray ionization– tandem mass spectrometry (LC-ESI-MS/MS). The results showed that the molecular mass of the purified peptide was 656.17 Da, and the amino acid sequence was Pro-Asn-Pro-Asn-Thr-Asn (PNPNTN). Splenocyte proliferation was 87.35% in the presence of 100 μg/ml of purified peptide. The splenocyte proliferation could be promoted upto 248.4% at 100 μg/ml of PNPNTN after induction by Concanavalin A (Con A). PNPNTN was stable in the presence of the gastrointestinal proteases pepsin and trypsin and at temperatures up to120°C. Taken together, these results show that this novel immunomodulatory hexapeptide from silkworm pupae has potential therapeutic value as an immunomodulatory component of functional food.
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