Bioavailability of corn gluten meal hydrolysates and their effects on the immune system
The bioavailability of food is central to human nutrition, health and wellbeing. Here, we tested the bioavailability of hydrolysed corn gluten meal using a protein efficiency ratio method, and then analysed differences in bodyweight, weight of organs, routine blood tests and histological sections. The results indicate that the average protein intake of the hydrolysed corn gluten meal (HCGM) group was higher than that of the crude corn gluten meal (CCGM) group, and was associated with an increase in average bodyweight. The corrected protein efficiency ratios (PERs) of the HCGM and CCGM groups were 0.374 and 0.217, respectively; the corrected PER of the HCGM group was 1.72 times higher than that of the CCGM group. These results show that hydrolysis increased the bioavailability of corn gluten meal. Furthermore, there was a significant difference in organ weights (salivary gland P < 0.01; thymus gland P < 0.05; spleen P < 0.01) between the HCGM and CCGM groups. Finally, no inf lammatory cell infiltrates nor cell necrosis could be found in any of the histological sections. We speculate that hydrolysed protein preparations can improve immunity.
Ai Yongfeng, Jane Jay-lin (2016): Macronutrients in Corn and Human Nutrition. Comprehensive Reviews in Food Science and Food Safety, 15, 581-598 https://doi.org/10.1111/1541-4337.12192
Anese Monica, Mirolo Giorgio, Beraldo Paola, Lippe Giovanna (2013): Effect of ultrasound treatments of tomato pulp on microstructure and lycopene in vitro bioaccessibility. Food Chemistry, 136, 458-463 https://doi.org/10.1016/j.foodchem.2012.08.013
Bhat Z. F., Kumar Sunil, Bhat Hina Fayaz (2015): Bioactive peptides of animal origin: a review. Journal of Food Science and Technology, 52, 5377-5392 https://doi.org/10.1007/s13197-015-1731-5
Boland Mike (2016): Human digestion - a processing perspective. Journal of the Science of Food and Agriculture, 96, 2275-2283 https://doi.org/10.1002/jsfa.7601
Filho C.B., Jesse C.R., Donato F., Giacomeli R., Del Fabbro L., da Silva Antunes M., de Gomes M.G., Goes A.T.R., Boeira S.P., Prigol M., Souza L.C. (2015): Chronic unpredictable mild stress decreases BDNF and NGF levels and Na+,K+-ATPase activity in the hippocampus and prefrontal cortex of mice: Antidepressant effect of chrysin. Neuroscience, 289, 367-380 https://doi.org/10.1016/j.neuroscience.2014.12.048
Grasso P. (2011): Novel approaches to the treatment of obesity and type 2 diabetes mellitus: Bioactive leptin-related synthetic peptide analogs. Recent Patents on Endocrine Metabolic & Immune Drug Discovery, 5: 163–175.
Jin J., Ma H., Qu W., Wang K ., Z hou C ., He R ., Luo L ., Owusu J. (2015a): Effects of multi-frequency power ultrasound on the enzymolysis of corn gluten meal: Kinetics and thermodynamics study. Ultrasonic Sonochemistry, 27: 46–53.
Jin J., Ma H., Zhou C., Luo M., Liu W., Qu W., He R., Luo L ., Yagoub A .E ..-G.A. (2015b): Effect of degree of hydrolysis on the bioavailability of corn gluten meal hydrolysates. Journal of the Science of Food and Agriculture, 95: 2501–2509.
Jin Jian, Ma Haile, Wang Bei, Yagoub Abu El-Gasim A., Wang Kai, He Ronghai, Zhou Cunshan (2016): Effects and mechanism of dual-frequency power ultrasound on the molecular weight distribution of corn gluten meal hydrolysates. Ultrasonics Sonochemistry, 30, 44-51 https://doi.org/10.1016/j.ultsonch.2015.11.021
Kadam S.U., Tiwari B.K., Álvarez C., O’Donnell C.P. (2015): Ultrasound applications for the extraction, identification and deliver y of food proteins and bioactive peptides. Trends in Food Science & Technology, 46: 60–67.
Li C.F., Chen X.M., Chen S.M., Mu R.H., Liu B.B., Luo L., Liu X.L., Geng D., Liu Q., Yi L.T. (2016a): Activation of hippocampal BDNF signaling is involved in the antidepressant-like effect of the NMDA receptor antagonist 7-chlorokynurenic acid. Brain Research, 1630: 73–82.
Li S., Yang X., Zhang Y., Ma H., Liang Q., Qu W., He R., Zhou C., Mahunu G.K . (2016b): Effects of ultrasound and ultrasound assisted alkaline pretreatments on the enzymolysis and structural characteristics of rice protein. Ultrasonics Sonochemistry, 31: 20–28.
Nooshkam Majid, Madadlou Ashkan (2016): Microwave-assisted isomerisation of lactose to lactulose and Maillard conjugation of lactulose and lactose with whey proteins and peptides. Food Chemistry, 200, 1-9 https://doi.org/10.1016/j.foodchem.2015.12.094
Norberg �., Gruber S., Angelucci F., Renlund S., Wadensten H., Efendic S., �stenson C.-G., J�rnvall H., Sillard R., Math� A. A. (2003): Identification of the bioactive peptide PEC-60 in brain. Cellular and Molecular Life Sciences (CMLS), 60, 378-381 https://doi.org/10.1007/s000180300030
Paddon-Jones Douglas, Rasmussen Blake B (2009): Dietary protein recommendations and the prevention of sarcopenia. Current Opinion in Clinical Nutrition and Metabolic Care, 12, 86-90 https://doi.org/10.1097/MCO.0b013e32831cef8b
Qu Wenjuan, Ma Haile, Jia Junqiang, He Ronghai, Luo Lin, Pan Zhongli (2012): Enzymolysis kinetics and activities of ACE inhibitory peptides from wheat germ protein prepared with SFP ultrasound-assisted processing. Ultrasonics Sonochemistry, 19, 1021-1026 https://doi.org/10.1016/j.ultsonch.2012.02.006
Qu Wenjuan, Ma Haile, Li Wen, Pan Zhongli, Owusu John, Venkitasamy Chandrasekar (2015): Performance of coupled enzymatic hydrolysis and membrane separation bioreactor for antihypertensive peptides production from Porphyra yezoensis protein. Process Biochemistry, 50, 245-252 https://doi.org/10.1016/j.procbio.2014.11.010
Julia Scerbo M., Bibolini Mario J., Barra José L., Roth German A., Monferran Clara G. (2008): Expression of a bioactive fusion protein of Escherichia coli heat-labile toxin B subunit to a synapsin peptide. Protein Expression and Purification, 59, 320-326 https://doi.org/10.1016/j.pep.2008.02.017
Tamayo Tenorio Angelica, Gieteling Jarno, de Jong Govardus A.H., Boom Remko M., van der Goot Atze J. (2016): Recovery of protein from green leaves: Overview of crucial steps for utilisation. Food Chemistry, 203, 402-408 https://doi.org/10.1016/j.foodchem.2016.02.092
Udenigwe Chibuike C., Aluko Rotimi E. (2012): Food Protein-Derived Bioactive Peptides: Production, Processing, and Potential Health Benefits. Journal of Food Science, 77, R11-R24 https://doi.org/10.1111/j.1750-3841.2011.02455.x
Wang Zhenbin, Lin Xiaoming, Li Pingping, Zhang Jie, Wang Shiqing, Ma Haile (2012): Effects of low intensity ultrasound on cellulase pretreatment. Bioresource Technology, 117, 222-227 https://doi.org/10.1016/j.biortech.2012.04.015
Yi Liya, Lakemond Catriona M.M., Sagis Leonard M.C., Eisner-Schadler Verena, van Huis Arnold, van Boekel Martinus A.J.S. (2013): Extraction and characterisation of protein fractions from five insect species. Food Chemistry, 141, 3341-3348 https://doi.org/10.1016/j.foodchem.2013.05.115
Yu H.-Ch., Wu J., Zhang H.-X., Zhang H.-S., Qiao T.-T., Zhang J.-X., Zhang G.-L., Sui J., Li L.-W., Zhang L.-R ., Lv L.-X. (2015a): Antidepressant-like and anti-oxidative efficacy of Campsis grandif lora flower. Journal of Pharmacy and Pharmacology, 67: 1705–1715.
Yu X., Zhou C., Yang H., Huang X., Ma H., Qin X., Hu J. (2015b): Effect of ultrasonic treatment on the degradation and inhibition cancer cell lines of polysaccharides from Porphyra yezoensis. Carbohydrate Polymers, 117: 650–656.
Zhang Yanyan, Ma Haile, Wang Bei, Qu Wenjuan, Li Yunliang, He Ronghai, Wali Asif (2015): Effects of Ultrasound Pretreatment on the Enzymolysis and Structural Characterization of Wheat Gluten. Food Biophysics, 10, 385-395 https://doi.org/10.1007/s11483-015-9393-4
Zhou Cunshan, Ma Haile, Ding Qingzhi, Lin Lin, Yu Xiaojie, Luo Lin, Dai Chunhua, Yagoub Abu El-Gasim A. (2013): Ultrasonic pretreatment of corn gluten meal proteins and neutrase: Effect on protein conformation and preparation of ACE (angiotensin converting enzyme) inhibitory peptides. Food and Bioproducts Processing, 91, 665-671 https://doi.org/10.1016/j.fbp.2013.06.003
Zhou Cunshan, Yu Xiaojie, Qin Xiaopei, Ma Haile, Yagoub Abu ElGasim A., Hu Jiali (2016): Hydrolysis of rapeseed meal protein under simulated duodenum digestion: Kinetic modeling and antioxidant activity. LWT - Food Science and Technology, 68, 523-531 https://doi.org/10.1016/j.lwt.2015.11.057
Zimmer Gert, Rohn Michael, McGregor Gerard P., Schemann Michael, Conzelmann Karl-Klaus, Herrler Georg (2003): Virokinin, a Bioactive Peptide of the Tachykinin Family, Is Released from the Fusion Protein of Bovine Respiratory Syncytial Virus. Journal of Biological Chemistry, 278, 46854-46861 https://doi.org/10.1074/jbc.M306949200