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Published on: June 10, 2022
Antioxidant peptides from corn gluten meal: Orthogonal design evaluation
Cunshan Zhou1, Jiali Hu2, Haile Ma1
1School of Food and Biological Engineering, Jiangsu University, No. 301 Xuefu Road, Zhenjiang 212013, China; Jiangsu Provincial Key Laboratory for Physical Processing of Agricultural Products, Jiangsu University, No. 301 Xuefu Road, Zhenjiang 212013, China; Jiangsu Provincial Research Center of Bio-process and Separation Engineering of Agri-products, Jiangsu University, No. 301 Xuefu Road, Zhenjiang 212013, China; Jiangsu Jiangda Five Pines Biotechnology Co., Ltd, No. 99 Jing 15 Road, Zhejiang 212009, China.
Optimized corn gluten meal hydrolysis peptides (CHP) exhibit enhanced antioxidant activity, particularly in scavenging hydroxyl radicals. This improvement is linked to increased oligopeptides and specific amino acids after enzymatic processing.
Area of Science:
- Food Science
- Biotechnology
- Biochemistry
Background:
- Corn gluten meal (CGM) is a protein-rich byproduct with potential for bioactive peptide production.
- Enzymatic hydrolysis is a common method for generating peptides with functional properties from protein sources.
- Optimizing hydrolysis conditions is crucial for maximizing the yield and bioactivity of peptides.
Purpose of the Study:
- To optimize the enzymatic hydrolysis of corn gluten meal (CGM) using Protamex.
- To characterize the resulting corn gluten meal hydrolysis peptides (CHP) for their molecular weight distribution and antioxidant activity.
- To identify the optimal processing parameters for enhancing the antioxidant properties of CHP.
Main Methods:
- An L16 (4(5)) orthogonal design was employed to optimize CGM concentration, heat pretreatment time, and enzymolysis pH, temperature, and time.
- Degree of hydrolysis (DH), undigested residue ratio, molecular weight (MW) distribution, and DPPH radical inhibition were key analysis indicators.
- Verification tests were conducted to assess the antioxidant capacity (hydroxyl radical scavenging and reducing power) of the optimized CHP.
Main Results:
- Optimal conditions were determined as 18% CGM concentration, 40 min heat pretreatment at 121 °C, and enzymolysis at pH 7.5, 55 °C for 24 hours.
- The optimized CHP demonstrated superior hydroxyl radical scavenging activity, followed by reducing power.
- Hydrolysis led to an increase in oligopeptides at the expense of di- and tripeptides, suggesting the formation of soluble aggregates from low MW peptides.
Conclusions:
- Optimized enzymatic hydrolysis effectively produced CHP with significant antioxidant properties.
- The enhanced antioxidant activity of CHP is associated with an increased DH, higher content of oligopeptides, Alanyl-Tyrosine, and antioxidant-related free amino acids.
- These findings highlight the potential of utilizing CGM for producing functional peptides with valuable antioxidant applications.
