Purification and Characterization of Antioxidant Peptides from Alcalase-Hydrolyzed Soybean (<i>Glycine</i> <i>max</i> L.) Hydrolysate and Their Cytoprotective Effects in Human Intestinal Caco-2 Cells

Zhang, Qiaozhi; Tong, Xiaohong; Li, Yang; Wang, Huan; Wang, Zhongjiang; Qi, Baokun; Sui, Xiaonan; Jiang, Lianzhou

doi:10.1021/acs.jafc.9b01235

Cited by 99 publications

(73 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Similar results have been shown in previous studies, such as SPH-I (Mw < 3 kDa) from the alcalase-hydrolyzed soybean hydrolysate (SPH) which decreased the death rate of injured Caco-2 cells induced by oxidative stress, increased CAT activity, and decreased MDA content [48]. Feng et al [49] reported that two peptides (TY and SGGY) from defatted walnut meal protein hydrolysates (DEMPH) had the protective effect against oxidative damage to SH-SY5Y cells, therefore SGGY could significantly increase cell viability, and improve GSH content at a concentration of 1.0 mg/mL (p < 0.01).…”

Section: Effect Of Mbphs-i On the Level Of Ros On Cellssupporting

confidence: 91%

Mung Bean Protein Hydrolysates Protect Mouse Liver Cell Line Nctc-1469 Cell from Hydrogen Peroxide-Induced Cell Injury

Xie

et al. 2019

Foods

View full text Add to dashboard Cite

Mung bean is nutritious and rich in protein (19.5%-33.1%). However, there are few studies on mung bean protein active peptides so the mung bean protein hydrolysates (MBPHs) were investigated for evaluating their ability to clear intracellular reactive oxygen species (ROS) and regulating the ability of antioxidant enzymes on NCTC-1469 cells. Results showed that MBPHs, MBPHs-I (molecular weight < 3 kDa), MBPHs-II (molecular weight between 3 and 10 kDa), and MBPHs-III (molecular weight > 10 kDa) could all improve the survival rate of cells compared with the model group. MBPHs, MBPHs-I, and MBPHs-II could significantly decrease the content of lactate dehydrogenase (LDH) and reduce the generation of malonaldehyde (MDA) at a concentration of 0.4 mg/mL. Regarding the intracellular ROS, the result showed that MBPHs-I significantly reduced the production of ROS (from 58.3% to 26.6%) and had a dose-dependent relationship. In addition, the amino acid analysis showed that MBPHs-I had a balanced amino acid composition. MBPHs-I is rich in lysine but was deficient in cereals. Therefore, the hydrophobic and aromatic amino acids in MBPHs-I were high, which could improve its antioxidant activity. According to the results, MBPHs-I was the best and most potent natural antioxidant and it can contribute to drug development and medical application.

show abstract

Section: Effect Of Mbphs-i On the Level Of Ros On Cellssupporting

confidence: 91%

Mung Bean Protein Hydrolysates Protect Mouse Liver Cell Line Nctc-1469 Cell from Hydrogen Peroxide-Induced Cell Injury

Xie

et al. 2019

Foods

View full text Add to dashboard Cite

show abstract

“…Then, protease inactivation was performed by heating the solution in water at 100 °C for 15 min. The protein solution was cooled to room temperature and then centrifuged at 10,000 g and 4 °C for 10 min to collect the supernatant containing MPH (Zhang et al., 2019).…”

Section: Methodsmentioning

confidence: 99%

“…The absorbance at 220 nm was monitored, and each eluate (10 min) was collected. The fractions with high absorbance were collected and applied for in vitro antioxidant activity assays (Zhang et al., 2019).…”

Section: Methodsmentioning

confidence: 99%

Purification and characterization of antioxidant peptides from enzymatic hydrolysate of mungbean protein

Xia

Song

Huang

et al. 2020

Journal of Food Science

View full text Add to dashboard Cite

In this study, the antioxidant activity of mungbean protein hydrolysate (MPH) was systematically investigated. MPH was fractionated by ultrafiltration into two major fractions (MPH‐1 <3 kDa, MPH‐2 >3 kDa). Fraction MPH‐1, which exhibited the highest antioxidant activity, was further fractionated by gel column into three fractions (MPH‐1A, MPH‐1B, and MPH‐1C). The antioxidant activity of the MPH‐1B fraction was stronger than that of the other fractions. Eight mungbean peptides (P1–P8) were identified in fraction MPH‐1B by UPLC‐Q‐TOF‐MS. Among them, peptides Trp‐Gly‐Asn (WGN, P2), Ala‐Trp (AW, P4), Arg‐Gly‐Trp‐Tyr‐Glu (RGWYE, P5), and Gly‐Val‐Pro‐Phe‐Trp (GVPFW, P7) had high antioxidant activity. Moreover, these four peptides exerted protective effects against H2O2‐induced cytotoxicity and regulated the MDA content, CAT activity, and total GSH content in HepG2 cells with specific observation. This study demonstrated the potential of MPH as a source of antioxidant peptides. This provides a scientific basis for the preparation of antioxidant peptides from mungbean protein. Practical Application This study demonstrated the potential of the hydrolysate of mungbean protein as a source of antioxidant peptides and provided a scientific basis for the preparation of antioxidant peptides from mungbean protein.

show abstract

“…This method was also regarded as simple, fast, and efficient for evaluating antioxidant activity, leading to its global use (Benzie et al, 1996;Canabady-Rochelle et al, 2015;Zhang, Tong et al, 2019). The same letter denotes that the variance of the two samples was not significant (p > .05); different letters denote that the variance of the two samples was significant (p < .05) FRAP method focused on the determination of the single-electron transfer from all kinds of ROS scavenging in this work.…”

Section: F I G U R Ementioning

confidence: 99%

“…FRAP method focused on the determination of the single-electron transfer from all kinds of ROS scavenging in this work. This method was also regarded as simple, fast, and efficient for evaluating antioxidant activity, leading to its global use (Benzie et al, 1996;Canabady-Rochelle et al, 2015;Zhang, Tong et al, 2019).…”

Section: Abtsmentioning

confidence: 99%

Double enzyme hydrolysis for producing antioxidant peptide from egg white: Optimization, evaluation, and potential allergenicity

Yuan

Zheng

et al. 2019

J Food Biochem

View full text Add to dashboard Cite

Egg white is a good source of high-quality proteins in food products and an excellent source of antioxidant active peptides through hydrolysis. The hydrolysis conditions for the preparation of potent antioxidant peptides from egg white with chymotrypsin and pepsin were optimized by the response surface methodology. The antioxidant activity and potential allergenicity of the prepared peptides were evaluated by the oxidative damage model and IgE-binding capability, respectively. After ultrafiltration, the peptide produced using the optimized parameters (preheating time of 3.16 hr, hydrolysis time of 3 hr, a sample/solution ratio of 10%, multiple enzymes ratio (E1/E2) of 1.7:1, and E/S of 0.4%) showed antioxidant activity of was 30.86 μmol AAE/g DW and with low potential for allergenicity. The optimized method is efficient and economical and may be applied to the industrial production of antioxidant peptides to obtain nutraceutical and pharmaceutical agents with low sensitivity. However, further in vivo studies must be conducted. Practical applicationsEgg is consumed as an excellent source of protein. Antioxidant peptides released from egg white is considered to be used in food preservation and human health.Few researches on the optimization of egg peptides were aimed to obtain practical techniques used in the food industry. In this paper, egg white hydrolysis peptide with high antioxidant property and low potential allergenicity was prepared after the optimization of double enzyme hydrolysis. The products could be a natural health care products derived from a dietary source and considered using in additive during food production and health food. And the methods used are economical and energysaving and could be developed to utilize in the food industry. K E Y W O R D S antioxidant peptide, egg white, hydrolysis, optimization S U PP O RTI N G I N FO R M ATI O N Additional supporting information may be found online in the Supporting Information section. How to cite this article: Yuan J, Zheng Y, Wu Y, Chen H, Tong P, Gao J. Double enzyme hydrolysis for producing antioxidant peptide from egg white: Optimization, evaluation, and potential allergenicity. J Food Biochem. 2020;44:e13113.

show abstract

Purification and Characterization of Antioxidant Peptides from Alcalase-Hydrolyzed Soybean (Glycine max L.) Hydrolysate and Their Cytoprotective Effects in Human Intestinal Caco-2 Cells

Cited by 99 publications

References 46 publications

Mung Bean Protein Hydrolysates Protect Mouse Liver Cell Line Nctc-1469 Cell from Hydrogen Peroxide-Induced Cell Injury

Mung Bean Protein Hydrolysates Protect Mouse Liver Cell Line Nctc-1469 Cell from Hydrogen Peroxide-Induced Cell Injury

Purification and characterization of antioxidant peptides from enzymatic hydrolysate of mungbean protein

Double enzyme hydrolysis for producing antioxidant peptide from egg white: Optimization, evaluation, and potential allergenicity

Contact Info

Product

Resources

About