Preparation and identification of antioxidant peptides from protein hydrolysate of marine alga Gracilariopsis lemaneiformis

Zhang, Xiaoqian; Cao, Dequn; Sun, Xue; Sun, Siqi; Xu, Nianjun

doi:10.1007/s10811-019-1746-9

Cited by 46 publications

(39 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…RSM has been widely used in condition optimization for producing antioxidant peptide from grass carp sarcoplasmic protein (Ren et al, 2008), corn gluten meal (Zhuang, Tang, Dong, Sun, & Liu, 2013), and egg white powder (Lin et al, 2013). In a similar work, chymotrypsin was shown to produce higher antioxidant peptides using the DPPH method and the enzymatic hydrolysis conditions were optimized using RSM (Zhang, Cao, et al, 2019). In our study, three axes of response surface were replaced by hydrolysis time, the ratio of enzyme 1 and enzyme 2, and the ratio of raw water and egg white, according to results of the pre-experiment.…”

Section: ) and The Enzyme-cutting Site Of Pepsin Is Mainly Aromamentioning

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

Section: ) and The Enzyme-cutting Site Of Pepsin Is Mainly Aromamentioning

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

show abstract

“…Various enzyme activities have been studied for their ability to release these BAPs and the hydrolysis conditions employed play a crucial role in determining the bioactive properties and potencies of the hydrolysates generated [67]. It is well documented that bioactive properties are affected by, e.g., enzyme:substrate, pH, temperature, hydrolysis duration as well as the enzyme inactivation conditions employed during the enzymatic hydrolysis of macroalgal proteins [37,50]. Furthermore, pre-treatment of macroalgae biomass/protein, such as drying, thermal treatment, or ultrasound has been reported to increase enzymatic hydrolysis rate leading to the optimization of BAP release [68].…”

Section: Generation Of Macroalgae-derived Bapsmentioning

confidence: 99%

“…Papain hydrolyzed U. lactuca possessed ACE and renin inhibitory activities (82.37 and 3.70%, respectively, when tested at 1 mg/mL) [71]. Different enzyme preparations (trypsin, pepsin, papain, α-chymotrypsin, Alcalase) were employed to generate Gracilariopsis lemaneiformis protein hydrolysates [37]. Among the enzymes used, the hydrolysate generated with α-chymotrypsin displayed the highest antioxidant activity.…”

Section: Generation Of Macroalgae-derived Bapsmentioning

confidence: 99%

“…Table 3 summarises the laboratory-scale application of membrane filtration in the processing of seaweed protein hydrolysates and BAPs. Some studies have reported the use of ultrafiltration centrifuge tubes, e.g., Amicon Ultra [37,81] or Macrosep Advance Centrifugal devices [29], whereas other studies have used cassette-type membranes with separate membrane systems, e.g., Millipore Labscale TFF system [82] to fractionate seaweed peptides. The advantages of membrane processing are that it is a well-established technique for protein/hydrolysate processing at a large scale, e.g., in dairy processing [83].…”

Section: Membrane Separationmentioning

confidence: 99%

“…In MS/MS, the compound is ionized, and the mass/charge (m/z) is detected in the first MS. Further selected parental ions with a specific m/z are then fragmented (commonly by collision-induced dissociation (CID) in an argon collider) and these fragmented ions are then analyzed by the second MS. As shown in Table 4, most of the studies in seaweed peptide identification have used LC-ESI-MS/MS coupled with different mass analyzers. While QTOF is the most frequently used [70,84,[94][95][96][97]100,101], ion trap or orbitrap analysers have also been employed in peptide mass analysis [37,73,91,102,103]. Matrix-assisted laser desorption/ionization (MALDI) is a system in which the sample is mixed with a matrix (e.g., α-cyano-4-hydroxytrans-cinnamic acid in 50% ACN containing 0.1% TFA [81]) and spotted in a stainless steel plate where it is evaporated until dryness and the test sample is subsequently ionized with a laser.…”

Section: Identification Of Bapsmentioning

confidence: 99%

See 2 more Smart Citations

Current knowledge on the extraction, purification, identification, and validation of bioactive peptides from seaweed

et al. 2020

View full text Add to dashboard Cite

Current knowledge on the extraction, purification, identification, and validation of bioactive peptides from seaweed Seaweed (macroalgae) is considered as a sustainable bioresource rich in high-quality nutrients such as protein. Seaweed protein can be used as an alternative to other protein sources. Furthermore, these proteins are natural reservoirs of bioactive peptides (BAPs) associated with various health benefits such as antioxidant, antihypertensive, and antidiabetic activities. However, seaweed-derived BAPs remain underexploited due to challenges that arise during protein extraction from algal biomass. Coupled with this, limited proteomic information exists regarding certain seaweed species. This review highlights the current state of the art of seaweed protein extraction techniques, e.g., liquid, ultrasound, microwave, pulsed electric field, and high hydrostatic pressure assisted extraction. The review also focuses on the enzymatic hydrolysis of seaweed proteins and characterization of the resultant hydrolysates/peptides using electrophoretic and chromatographic techniques. This includes reference to methods employed for separation, fractionation, and purification of seaweed BAPs, as well as the methodologies used for identification, e.g., analysis by mass spectrometry. Furthermore, a bioinformatics or in silico approach to aid discovery of seaweed BAPs is discussed herein. Based on the information available to date, it is suggested that further research is required in this area for the development of seaweed BAPs for nutraceutical applications.

show abstract

HPLC purification of antioxidant and antibacterial peptides from a lichen “Parmotrema perlatum (Huds.) M. Choisy”: Identification by LC‐MS/MS peptide mass fingerprinting

Radhakrishnan,

Kanakaraja,

Krishnan

et al. 2024

Biotech and App Biochem

View full text Add to dashboard Cite

Parmotrema perlatum, a lichen belonging to the family Parmeliaceae, is well known for its culinary benefits and aroma used as a condiment in Indian homes is also known as the “black stone flower” or “kalpasi” in India. This research intends to analyze the antioxidant power of the crude extracts using four pH‐based buffers solubilized proteins/peptides and RP‐HPLC fractions of P. perlatum obtained by purification. The proteins that were extracted from the four different buffers were examined using LC‐MS/MS‐based peptide mass fingerprinting. When compared to the other buffers, the 0.1 M of Tris‐HCl buffer pH 8.0 solubilized proteins/peptides had the strongest antioxidant capacity. The sequential purification of the peptide was carried out by using a 3‐kDa cut‐off membrane filter and semipreparative RP‐HPLC. Additionally, the purified fractions of the peptide's antioxidant activity were assessed, and effects were compared with those of the crude and 3 kDa cut‐‐off membrane filtrates. The peptide fractions were sequenced by LC‐MS/MS, which reveals that fraction 2 from RP‐HPLC with the sequence LSWFMVVAP has shown the highest antioxidant potential in comparison with other fractions which can serve as the potential natural antioxidant drug. Further, fraction 2 also showed antibacterial activity against the selected microorganisms.

show abstract

Preparation and identification of antioxidant peptides from protein hydrolysate of marine alga Gracilariopsis lemaneiformis

Cited by 46 publications

References 42 publications

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

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

Current knowledge on the extraction, purification, identification, and validation of bioactive peptides from seaweed

HPLC purification of antioxidant and antibacterial peptides from a lichen “Parmotrema perlatum (Huds.) M. Choisy”: Identification by LC‐MS/MS peptide mass fingerprinting

Contact Info

Product

Resources

About