Production of Fermentative Hydrolysate with Antioxidative Activity of Extruded Corn Gluten Meal by Bacillus natto

Abstract:

Fermentative hydrolysate of extruded corn gluten with higher solubility and antioxidative property by Bacillus natto was prepared. Extrusion of corn gluten was applied as pretreatment before fermentation. The best fermentative hydrolysis results can be obtained by fermenting at 34°C for cultivation time of 32 h, and flask rotation speed and initial pH of culture media were 200 r/min and 6.5-7.0 respectively. Soluble protein content and antioxidative activity of the fermentative hydrolysate reached 24.95 mg/ml and 259.21 U/ml respectively under the optimized culture condition. The molecular weight of the peptides in the optimal hydrolysate distributed mainly over 860-5300 Da determined by gel filtration chromatography. The hydrolysates displayed good solubility and antioxidative activity.

• Periodical: Applied Mechanics and Materials (Volumes 138-139)
• Pages: 1142-1148
• DOI: https://doi.org/10.4028/www.scientific.net/AMM.138-139.1142
• Online since: November 2011
• Authors: Xi Qun Zheng, Xiao Lan Liu, Zhi Sheng Liu
• Keywords: Antioxidative Activity, Bacillus natto, Corn Gluten, Extrusion, Fermentation, Hydrolysate

References

[1] M. A. Dombrink-Kurtzman, and J. A. Bietz, Zein composition in hard and soft endosperm of maize, Cereal Chem, vol. 70, no. 1, pp.105-108, January-February (1993).

[2] K. Surówka, D. Żmudziński, and J. Surówka, Enzymic modification of extruded soy protein concentrates as a method of obtaining new functional food components, Trends in Food Science & Technology, vol. 15, no. 3-4, pp.153-160, March-April (2004).

DOI: 10.1016/j.tifs.2003.09.013

[3] F. G. Bernard, Z. Alexandre, M. Robert, and M. Catherine, Production and characterization of bioactive peptides from soy hydrolysate and soy-fermented food, Food Research International, vol 37, no. 2, pp.123-131, March (2004).

DOI: 10.1016/j.foodres.2003.09.010

[4] M. Darewicz, J. Dziuba, and P.W.J.R. Caessens, Effect of enzymatic hydrolysis on emusifying and foaming properties of milk proteins—a review, Polish Journal of Food and Nutrition Sciences, vol. 9, no. 1, pp.3-8, January (2002).

[5] J. M. Kim, J. H. Whang, K. M. Kim, J. H. Koh, and H. J. Suh, Preparation of corn gluten hydrolysate with angiotensin I converting enzyme inhibitory activity and its solubility and moisture sorption, Process Biochemistry, vol. 39, no. 8, pp.989-994, April (2004).

DOI: 10.1016/s0032-9592(03)00205-x

[6] H. J. Suh, J. H. Whang, D.B. Suh, S.H. Bae, and D. O. Noh, Preparation of angiotensin I converting enzyme inhibitory from corn gluten, Process Biochemistry, vol. 38, no. 8, pp.1239-1244, March (2003).

DOI: 10.1016/s0032-9592(02)00316-3

[7] H. Y. Zheng, Anti-fatigue effect of corn peptide, Journal of the Chinese Cereals and Oils Association, vol. 20, no. 1, pp.33-35, February (2005).

[8] M. Pan, T. S. Jiang, and J. L. Pan, Antioxidant activities of rapeseed protein hydrolysates, Food Bio-process Technol, DOI 10. 1007/s11947-009-0206-y, April (2009).

[9] A. P. Adebiyi, A. O. Adebiyi, J. Yamashita, T. Ogawa, and K. Muramoto, Purification and characterization of antioxidative peptides derived from rice bran protein hydrolysates, Eur Food Res Technol, vol. 228, no. 4, pp.553-563, February (2009).

DOI: 10.1007/s00217-008-0962-3

[10] J. H. Zhang, H. Zhang, L. Wang, X. N. Guo, X. G. Wang, and H. Y. Yao, "Antioxidant activities of the rice endosperm protein hydrolysate: identification of the active peptide. Eur Food Res Technol, vol. 229, no. 4, pp.709-719, August (2009).

DOI: 10.1007/s00217-009-1103-3

[11] X. X. Lu, X. H. Chen, and J. Z. Tang, Studies on the functional property of enzymatic modified corn protein, Food Science, vol. 21, no. 12, pp.13-15, December (2000).

[12] H. Sumi, H. Hamada, H. Tsushima, H. Mihara, and H. Muraki, A novel fibrinolytic enzyme (Nattokinase) in the vegetable cheese Natto, a typical and popular soybean food in the Japanese diet, Experientia, vol. 43, no. 10, pp.1110-1111, October (1987).

DOI: 10.1007/bf01956052

[13] O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, Protein measurement with the Folin phenol reagent, Journal of Biological Chemistry, vol. 193, no. 1, pp.264-275, November (1951).

DOI: 10.1016/s0021-9258(19)52451-6

[14] U. K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, vol. 227, no. 5259, pp.680-686, August (1970).

DOI: 10.1038/227680a0

[15] S. Marklund, and G. Marklund, Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase, Eur J Biochem, vol. 47, no. 3, pp.469-474, September (1974).

DOI: 10.1111/j.1432-1033.1974.tb03714.x

[16] S. H. Prudêncio-Ferreira, and J. A. G Arêas, Protein-protein interactions in the extrusion of soya at various temperatures and moisture contents, Journal of Foods Science, vol. 58, no. 2, pp.378-381 (384), March (1993).

DOI: 10.1111/j.1365-2621.1993.tb04279.x

[17] X. Q. Zheng, L. L. Li, X. L. Liu, X. J. Wang, J. Lin, and D. Li, Production of hydrolysate with antioxidative activity by enzymatic hydrolysis of extruded corn gluten, Applied Microbiology and Biotechnology, vol. 73, no. 4, pp.763-770, December (2006).

DOI: 10.1007/s00253-006-0537-9

[18] J. Y. Wang, K. Fujimoto, T. Miyazawa, and Y. Endo, Anti-oxidative mechanism of maize zein in powder model systems against methyl linoleate: effect of water activity and coexistence of antioxidants, J Agric Food Chem. vol. 39, no. 2, pp.351-355.

DOI: 10.1021/jf00002a025