Enzymic hydrolysis of corn gluten meal

Hardwick, Julie Elizabeth; Glatz, Charles E.

doi:10.1021/jf00088a081

Cited by 24 publications

(9 citation statements)

References 12 publications

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“…2006). However, very little is known about the antioxidant capacity of corn peptides (CPS), hydrolyzate of corn ( Zea mays ) gluten meal, a by‐product of the corn wet‐milling process containing approx 60% protein (Hardwick and Glatz 1989).…”

Section: Introductionmentioning

confidence: 99%

“…Recently, antioxidant activities of some protein hydrolyzates have been described, such as Pollack skin gelatin (Kim et al 2001), round scad (Thiansilakul et al 2007) and yellow stripe trevally (Klompong et al 2007), wheat gluten (Wang et al 2007) and wheat germ protein (Zhu et al 2006). However, very little is known about the antioxidant capacity of corn peptides (CPS), hydrolyzate of corn (Zea mays) gluten meal, a by-product of the corn wet-milling process containing approx 60% protein (Hardwick and Glatz 1989).…”

Section: Introductionmentioning

confidence: 99%

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Antioxidant Properties and Possible Mode of Action of Corn Protein Peptides and Zein Peptides

Guo

et al. 2010

Journal of Food Biochemistry

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Corn peptides (CPS) and zein peptides (ZPS) were prepared from defatted corn gluten meal and zein, respectively by proteolysis with alcalase, an alkaline protease. The molecular‐mass distributions and amino acid compositions of CPS and ZPS were determined and compared. With α‐tocopherol as the positive control, the antioxidant activities of CPS and ZPS were investigated by several in vitro assay systems, including the scavenging effects on 2, 2‐diphenyl‐1‐picrylhydrazyl radical, the inhibiting emergence of hydroxyl radical and prevention of linoleic acidauto‐oxidation and the reducing power of CPS and ZPS. The capacities of CPS and ZPS removing superoxide anion from pyrogallol auto‐oxidation were also estimated. The data revealed that the antioxidant potency of CPS was similar to that of ZPS. CPS and ZPS also exhibited the similar reducing power. The possible mode of action of antioxidant activity was because of the presence of some proton‐donating peptide components in CPS and ZPS products. PRACTICAL APPLICATIONS CPS, hydrolyzate of corn gluten meal through the action of alcalase with the molecular‐mass distribution from 300 to 1,000 Da, showed the same notable antioxidant activities, free radical‐scavenging activities and reducing power in vitro as those of ZPS, hydrolyzate of zein. Therefore, CPS rather than ZPS can be used as an ingredient with antioxidant activity in pharmaceutical and food industries in the future. Subsequently, the cost of production of natural antioxidant can be decreased and the process of production also be simplified greatly.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Antioxidant Properties and Possible Mode of Action of Corn Protein Peptides and Zein Peptides

Guo

et al. 2010

Journal of Food Biochemistry

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Cereal Chem. The improvement of the functional properties of proteins by enzymatic or chemical modifications has been extensively studied (Hardwick and Glatz 1989, Hamada 1992, Guillerme et al 1993, Guéguen et al 1995, Chobert et al 1996.Wheat gluten, a by-product of the wheat starch industry, is a typical water-insoluble protein. Reversed-phase HPLC analysis of gluten hydrolysates with a degree of hydrolysis (DH) in the range of 0-5% showed that both hydrophilic and hydrophobic soluble peptides were released.

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confidence: 99%

Emulsifying and Foaming Properties of Gluten Hydrolysates with an Increasing Degree of Hydrolysis: Role of Soluble and Insoluble Fractions

Linarès

Larré

Lemeste³

et al. 2000

Cereal Chem

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Cereal Chem. 77(4): [414][415][416][417][418][419][420] Gluten solubility was improved by enzymatic proteolysis at moderate acidic pH level. Reversed-phase HPLC analysis of gluten hydrolysates with a degree of hydrolysis (DH) in the range of 0-5% showed that both hydrophilic and hydrophobic soluble peptides were released. Emulsifying and foaming properties of hydrolysate dispersions at 3.75 mg/mL decreased with the increasing DH at all pH levels and salt conditions investigated.On the other hand, the soluble fractions separated from those hydrolysate dispersions exhibited good functional properties, independently of the initial DH. The proportion of hydrophilic and hydrophobic peptides in the soluble fractions depended on DH, pH level, and salt concentration. Nevertheless, these soluble fractions were characterized by an excellent capacity to stabilize both oil-water and air-water interfaces.The solubility properties of proteins, which depend on intrinsic physicochemical characteristics and on the pH level and salt conditions of the medium, sometimes limit their use in formulated food systems (Panyam and Kilara 1996). The improvement of the functional properties of proteins by enzymatic or chemical modifications has been extensively studied (Hardwick and Glatz 1989, Hamada 1992, Guillerme et al 1993, Guéguen et al 1995, Chobert et al 1996.Wheat gluten, a by-product of the wheat starch industry, is a typical water-insoluble protein. Much research focused on chemical or enzymatic modifications has resulted in the enhancement of its solubility, foaming, and emulsifying properties (Yang and McCalla 1968, Batey 1985, Bollecker et al 1990, Thébaudin 1990, Kato et al 1991, Mannheim and Cheryan 1992, Mimouni et al 1994, Babiker et al 1996. Adler-Nissen (1986) reported that extensive protein hydrolysis produced short peptides unable to form stable films at the oil-water or air-water interfaces. Thébaudin (1990) showed that limited hydrolysis of wheat proteins by various proteases improved solubility and that gluten hydrolysates with a degree of hydrolysis (DH) in the range of 1-2% exhibited good emulsifying and foamforming properties. However, the foam-stabilizing properties of gluten hydrolysates were very limited (Thébaudin 1990, Mannehein andCheryan 1992). Proteolysis of gluten by several enzymes (pepsin, neutrase, alcalase) confirmed these results (Mimouni et al 1994). According to this author, a pepsin hydrolysate with 1.25% DH exhibited a solubility of 80% but poor foam-stabilizing properties at pH 7. This showed that high solubility is not the only requirement to improve other functional properties. It is important to note that many studies were performed with total hydrolysates characterized by high solubility but only a few reported the effect of the insoluble fraction. Only Velev et al (1993) compared the emulsifying properties of tomato seed protein isolate with its water-soluble fraction and noted a positive effect of the insoluble fraction.The objectives of this research were 1) to study the hydrolysis of gl...

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“…Relative to the extraction yields of as-is zein, the extraction yields of zein from extruded CGM did not change greatly, but the extraction yields of zein from CGM treated with extrusion and starch removal was lower. Zein accounts for about 65% of the total protein of CGM (Neumann et al 1984;Hardwick and Glatz 1989), so the total extraction yields in Table I indicate that about 75% of zein in as-is CGM was obtained after extraction, whereas about 58% of zein in CGM treated with extrusion and starch removal was obtained after extraction. The starch removal process facilitated by α-amylase decreased the zein extraction yield significantly compared with the control.…”

Section: Effect Of Pretreatment On the Extraction Yield Of Zeinmentioning

confidence: 99%

“…Corn gluten meal (CGM) is a major coproduct of the corn wetmilling process, and CGM contains approximately 62-71% (w/w) protein and 21-26% (w/w) carbohydrate, of which 12-15% (w/w) is starch (Dombrink-Kurtzman and Bietz 1993); it is mostly utilized as an animal feed. Zein is a major protein fraction of CGM and constitutes up to 65-68% of the total protein (Neumann et al 1984;Hardwick and Glatz 1989). It has been previously reported that zein has special functional amino acid sequences with antioxidative activity (Zheng et al 2006;Zhang et al 2011;Zhou et al 2012), angiotensin I converting enzyme-inhibitory activity (Suh et al 1999(Suh et al , 2003, and facilitating alcohol metabolism activity (Ma et al 2012).…”

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confidence: 99%

Effects of Extrusion and Starch Removal Pretreatment on Zein Proteins Extracted from Corn Gluten Meal

Zheng

Liu

et al. 2014

Cereal Chem

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In this study, the structure and selected properties of zeins extracted from corn gluten meal (CGM) pretreated by extrusion and removal of starch were investigated. The structure and properties of the zeins from pretreated CGM changed significantly. Pretreatments can decrease the extraction yields of zeins and change the granule shape and size of zein aggregates. The studies indicated that extrusion and removal of starch can significantly decrease the thermal enthalpy (ΔH1 and ΔH2) of zein from 1.94 ± 0.20 to 0.19 ± 0.10 and from 107.20 ± 0.80 to 78.62 ± 2.30 and J/g, respectively. The SDS‐PAGE results confirmed that the molecular weight of zeins from CGM was 24,000 and 27,000, and the molecular weight of zeins did not change with the pretreatment. On the other hand, the circular dichroism spectroscopy results showed that the processing of extrusion and removal of starch can change the secondary structure content of β‐sheets and β‐turns; these results indicated that extrusion and removal of starch can significantly break the secondary structure of zeins. Furthermore, extrusion and removal of starch can change the sulfhydryl content of zeins. The obtained results provided some fundamental information that is useful for further modification of CGM to improve its functional properties and industrial applications.

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Enzymic hydrolysis of corn gluten meal

Cited by 24 publications

References 12 publications

Antioxidant Properties and Possible Mode of Action of Corn Protein Peptides and Zein Peptides

Antioxidant Properties and Possible Mode of Action of Corn Protein Peptides and Zein Peptides

Emulsifying and Foaming Properties of Gluten Hydrolysates with an Increasing Degree of Hydrolysis: Role of Soluble and Insoluble Fractions

Effects of Extrusion and Starch Removal Pretreatment on Zein Proteins Extracted from Corn Gluten Meal

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