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Comparisons of Processing Stability and Antioxidant Activity of the Silkworm Pupae Protein Hydrolysates by Spray-dry and Freeze-dry

  • Chuanchao Shi , Zehua Lin , Xiaochun Xiao , Xufeng Zhai , Chung Wah Ma and Jiaoyan Ren EMAIL logo
Published/Copyright: December 12, 2017

Abstract

Silkworm pupae protein (SPP) was pretreated by different processing (heat/alkali/pepsin) and then hydrolyzed by five proteases (trypsin/flavorzyme/papain/protamex/alcalase), respectively. It was found that the combination of heat pretreatment and alkali pretreatment followed by enzymatic hydrolysis with trypsin and flavorzyme could remarkably improve the protein recovery. The hydrolysates obtained from silkworm pupae protein hydrolyzed with trypsin and flavorzyme were stable at the pH range of 4.0–8.0, remaining 95 % of its original reducing power and 90 % of its OH• scavenging activity. However, they were susceptible to alkaline treatments (pH > 10.0) and lost >30 % of their antioxidant activities. Pasteurization (65 °C × 30 min) or autoclaving sterilization (121 °C × 20 min) did not show notable effects on the antioxidant activities. It was concluded that silkworm pupae protein hydrolysates (SPPH) were better to be applied in either neutral or acidic food system rather than in alkaline conditions.

Acknowledgments

The authors gratefully acknowledge the Guangdong Natural Science Funds for Distinguished Young Scholars (S2013050013954), Program for New Century Excellent Talents in University (NCET-13-0213), Guangdong Special Funding for Outstanding Young Scholars (2014TQ01N645), Guangdong Science and Technology Planning Project (2015A010107003), Fundamental Research Funds for the Central Universities (2015PT015) and the Students Research Funding of Guangdong Province (pdjh2016b0049).

Disclosure statement

No potential conflict of interest was reported by the authors.

References

[1] Behera P, Kumar R, Sandeep IV, Kapila R, Dang AK, Kapila S. Casein hydrolysates enhance osteoblast proliferation and differentiation in mouse bone marrow culture. Food Biosci. 2013;2:24–30.10.1016/j.fbio.2013.03.008Search in Google Scholar

[2] de Castro RJ, Sato HH. Biologically active peptides: processes for their generation, purification and identification and applications as natural additives in the food and pharmaceutical industries. Food Res Int. 2015;74:185–98.10.1016/j.foodres.2015.05.013Search in Google Scholar

[3] Ren J, Zhao M, Shi J, Wang J, Jiang Y, Cui C, et al.. Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry. Food Chem. 2008;2:727–36.10.1016/j.foodchem.2007.11.010Search in Google Scholar

[4] Nikoo M, Benjakul S. Potential application of seafood-derived peptides as bifunctional ingredients, antioxidant–cryoprotectant: a review. J Funct Foods. 2015;19:753–64.10.1016/j.jff.2015.10.014Search in Google Scholar

[5] Nongonierma AB, FitzGerald RJ. The scientific evidence for the role of milk protein-derived bioactive peptides in humans: a Review. J Funct Foods. 2015;17:640–56.10.1016/j.jff.2015.06.021Search in Google Scholar

[6] Ameri M, Maa YF. Spray drying of biopharmaceuticals: stability and process considerations. Drying Technol. 2006;6:763–68.10.1080/03602550600685275Search in Google Scholar

[7] Murugesan R, Orsat V. Spray drying for the production of nutraceutical ingredients – a review. Food Bioprocess Technol. 2012;1:3–14.10.1007/s11947-011-0638-zSearch in Google Scholar

[8] Verma A, Singh SV. Spray drying of fruit and vegetable juices – a review. Crit Rev Food Sci Nutr. 2015;5:701–19.10.1080/10408398.2012.672939Search in Google Scholar

[9] Ratti C. Hot air and freeze-drying of high-value foods: a review. J Food Eng. 2001;4:311–19.10.1016/S0260-8774(00)00228-4Search in Google Scholar

[10] James C, Purnell G, James S. A review of novel and innovative food freezing technologies. Food Bioprocess Technol. 2015;8:1616–34.10.1007/s11947-015-1542-8Search in Google Scholar

[11] Zhou J, Han D. Proximate, amino acid and mineral composition of pupae of the silkworm Antheraea pernyi in China. J Food Composition Anal. 2006;8:850–53.10.1016/j.jfca.2006.04.008Search in Google Scholar

[12] Zhou J, Han D. Safety evaluation of protein of silkworm (Antheraea pernyi) pupae. Food Chem Toxicol. 2006;7:1123–30.10.1016/j.fct.2006.01.009Search in Google Scholar

[13] Deori M, Boruah DC, Devi D, Devi R. Antioxidant and antigenotoxic effects of pupae of the muga silkworm Antheraea assamensis. Food Biosci. 2014;5:108–14.10.1016/j.fbio.2013.12.001Search in Google Scholar

[14] Liao L, Wang Q, Zhao MM. Functional, conformational and topographical changes of succinic acid deamidated wheat gluten upon freeze-and spray-drying: a comparative study. LWT Food Sci Technol. 2013;1:177–84.10.1016/j.lwt.2012.06.002Search in Google Scholar

[15] Horowitz W. Official methods of analysis. Washington, DC: AOAC, 1970:17–18. Official methods of analysis.Search in Google Scholar

[16] Benjakul S, Morrissey MT. Protein hydrolysates from Pacific whiting solid wastes. J Agric Food Chem. 1997;9:3423–30.10.1021/jf970294gSearch in Google Scholar

[17] Li Y, Jiang B, Zhang T, Mu W, Liu J. Antioxidant and free radical-scavenging activities of chickpea protein hydrolysate (CPH). Food Chem. 2008;2:444–50.10.1016/j.foodchem.2007.04.067Search in Google Scholar

[18] Wu HC, Chen HM, Shiau CY. Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus). Food Res Int. 2003;9:949–57.10.1016/S0963-9969(03)00104-2Search in Google Scholar

[19] Zhang Y, Olsen K, Grossi A, Otte J. Effect of pretreatment on enzymatic hydrolysis of bovine collagen and formation of ACE-inhibitory peptides. Food Chem. 2013;3:2343–54.10.1016/j.foodchem.2013.05.058Search in Google Scholar PubMed

[20] Lin S, Tian W, Li H, Cao J, Jiang W. Improving antioxidant activities of whey protein hydrolysates obtained by thermal preheat treatment of pepsin, trypsin, alcalase and flavourzyme. Int J Food Sci Tech. 2012;10:2045–51.10.1111/j.1365-2621.2012.03068.xSearch in Google Scholar

[21] Faithong N, Benjakul S, Phatcharat S, Binsan W. Chemical composition and antioxidative activity of Thai traditional fermented shrimp and krill products. Food Chem. 2010;1:133–40.10.1016/j.foodchem.2009.06.056Search in Google Scholar

[22] Lapsongphon N, Yongsawatdigul J. Production and purification of antioxidant peptides from a mungbean meal hydrolysate by Virgibacillus sp. SK37 proteinase. Food Chem. 2013;2:992–99.10.1016/j.foodchem.2013.04.054Search in Google Scholar

[23] Korhonen H, Pihlanto-Leppäla A, Rantamäki P, Tupasela T. Impact of processing on bioactive proteins and peptides. Trends Food Sci Technol. 1998;8:307–19.10.1016/S0924-2244(98)00054-5Search in Google Scholar

[24] Nalinanon S, Benjakul S, Kishimura H, Shahidi F. Functionalities and antioxidant properties of protein hydrolysates from the muscle of ornate threadfin bream treated with pepsin from skipjack tuna. Food Chem. 2011;4:1354–62.10.1016/j.foodchem.2010.07.089Search in Google Scholar

[25] Kittiphattanabawon P, Benjakul S, Visessanguan W, Shahidi F. Gelatin hydrolysate from blacktip shark skin prepared using papaya latex enzyme: antioxidant activity and its potential in model systems. Food Chem. 2012;3:1118–26.10.1016/j.foodchem.2012.05.080Search in Google Scholar

[26] Li X, Luo Y, You J, Shen H. Stability of papain-treated grass carp (Ctenopharyngodon idellus) protein hydrolysate during food processing and its ability to inhibit lipid oxidation in frozen fish mince. J Food Sci Technol. 2013;52:542–48.10.1007/s13197-013-1031-xSearch in Google Scholar

[27] Sikorski ZE, Naczk M, Toledo RT. Modification of technological properties of fish protein concentrates. Crit Rev Food Sci Nutr. 1981;3:201–30.10.1080/10408398109527305Search in Google Scholar

[28] Li Y-W LB. Characterization of structure–antioxidant activity relationship of peptides in free radical systems using QSAR models: key sequence positions and their amino acid properties. J Theor Biol. 2013;318:29–43.10.1016/j.jtbi.2012.10.029Search in Google Scholar

[29] Foegeding EA, Davis JP, Doucet D, McGuffey MK. Advances in modifying and understanding whey protein functionality. Trends Food Sci Technol. 2002;5:151–59.10.1016/S0924-2244(02)00111-5Search in Google Scholar

[30] Linares E, Larré C, Popineau Y. Freeze-or spray-dried gluten hydrolysates. 1. Biochemical and emulsifying properties as a function of drying process. J Food Eng. 2001;2:127–35.10.1016/S0260-8774(00)00148-5Search in Google Scholar

[31] Chen C, Chi YJ, Xu W. Comparisons on the functional properties and antioxidant activity of spray-dried and freeze-dried egg white protein hydrolysate. Food Bioprocess Technol. 2012;6:2342–52.10.1007/s11947-011-0606-7Search in Google Scholar

Received: 2016-7-27
Accepted: 2017-11-23
Published Online: 2017-12-12

© 2018 Walter de Gruyter GmbH, Berlin/Boston

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