Tri‐ and dipeptides identification in whey protein and porcine liver protein hydrolysates by fast LC–MS/MS neutral loss screening and <i>de novo</i> sequencing

Poliseli, Camila B.; Tonin, Angélica Priscila Parussolo; Martinez, Fernanda C.; Nascimento, Nicholas C. do; Braz, Vilmar; Maluf, José Uebi; Ribeiro, Valquíria; Rosa, Fernanda A.; Souza, Gustavo H.M.F.; Meurer, Eduardo C.

doi:10.1002/jms.4701

Cited by 4 publications

(4 citation statements)

References 41 publications

(31 reference statements)

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“…In the present study, the rapid LC‐MS/MS method based on the neutral loss (NL) of 46 Da (CO and H 2 O or formic acid) was used, with the main objective of identifying di and tripeptides obtained from soy protein from enzymatic hydrolysis. The system used consists of rapid tracking (5 min) of protonated di‐ and tripeptide molecules, in which there is a selective neutral loss (NL) of 46 Da, due to the carboxylic acid portion and also comprises the search for dissociation fragments collision‐induced (CID) by de novo sequencing (Poseli et al ., 2021).…”

Section: Resultsmentioning

confidence: 99%

“…The bioactive peptides of the hydrolysates were analysed as described by Poseli et al . (2021), using a Quattro Premier XE triple‐quadrupole mass spectrometer (Waters Corporation, Milford, MA, The USA) equipped with an electrospray ionisation source, a Waters 515 pump and an XBridge (Waters) C18 3.5 μm (4.6 × 50 mm) column. For sample preparation, 0.1 g of hydrolysed was dissolved in 1 mL of 50 m m ammonium bicarbonate solution.…”

Section: Methodsmentioning

confidence: 99%

“…However, the techniques commonly used to investigate the smallest peptides (di‐ or tri‐) have the disadvantage of time‐consuming sample preparation and the need for chromatographic fractionation. Liquid chromatography (LC) coupled with tandem mass spectrometry (MS/MS) has been frequently selected for the identification of biopeptides in complex mixtures (Poseli et al ., 2021).…”

Section: Introductionmentioning

confidence: 99%

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Obtaining of bioactive di‐ and tripeptides from enzymatic hydrolysis of soybean meal and its protein isolate using Alcalase® and Neutrase®

Crozatti

Miyoshi

Tonin

et al. 2022

Int J of Food Sci Tech

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The obtaining of bioactive di-and tripeptides using AlcalaseÒ and NeutraseÒ enzymes in the hydrolysis of soybean meal (SM) and its protein isolate (SPI) was evaluated. An innovative system by fast LC-MS/ MS neutral loss screening and de novo sequencing was used to identify bioactive peptides. Soy protein characterisation, gel electrophoresis and antioxidant activity of the obtained peptides were performed. Results achieved showed that the use of AlcalaseÒ and SPI preparation potentiated the peptide breaking bonds and favoured the obtainment of bioactive peptides. The antioxidant activity of tested samples was significantly improved with enzymatic hydrolysis. LC-MS/MS analyses identified nineteen peptides in SM and 51 in SPI, all obtained after hydrolysis with AlcalaseÒ and, according to BIOPEP, with relevant bioactivities and expressive functional potential. Therefore, it is suggested that bioactive peptides achieved in this study can enable the development of new ingredients and provide greater added value to soy byproducts.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Obtaining of bioactive di‐ and tripeptides from enzymatic hydrolysis of soybean meal and its protein isolate using Alcalase® and Neutrase®

Crozatti

Miyoshi

Tonin

et al. 2022

Int J of Food Sci Tech

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“…The amino acids were analyzed according to Poliseli et al [ 20 ]. For sample preparation, 0.10 g of protein isolate from the asparagus by-product was dissolved in 1.0 mL of 50 mM ammonium bicarbonate solution.…”

Section: Methodsmentioning

confidence: 99%

Optimization and Characterization of Protein Extraction from Asparagus Leafy By-Products

dos Santos-Silva,

Saraiva,

Lazzari

et al. 2024

Foods

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Asparagus production generates significant amounts of by-products during the summer and post-harvest growth period. By-products can be good sources of nutrients and phytochemicals. The interest in increasing the availability of proteins for human consumption has led to the use of new plant sources rich in proteins. The objective of this study was to use response surface methodology (RSM) to optimize the aqueous extraction process of proteins from asparagus leafy by-products, for the production of new protein ingredients. The optimum extraction condition was at pH 9, with 40 min of extraction at 50 °C, and the concentration was fixed at 5 g·L−1. The isolate obtained presented 90.48% protein with 43.47% protein yield. Amino acids such as alanine, proline, valine, leucine/isoleucine, asparagine, and phenylalanine were identified, and the antioxidant activity for 2,2 AZINO BIS (3-ethylbenzo thiazoline 6 sulfonic acid diammonium salt) was 145.76 equivalent to Trolox μmol.100g.−1 and for DPPH 65.21 equivalent to Trolox μmol.100g.−1. The product presented favorable technological properties (water absorption capacity 4.49 g·g−1 and oil absorption capacity 3.47 g·g−1) and the color tended towards dark green (L* 31.91, a* −1.01, b* −2.11). The protein isolate obtained through the extraction optimization process showed high potential to be used as a protein ingredient.

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Study of the Antioxidant, Antimicrobial, and Wound Healing Properties of Raw Hydrolyzed Extract from Nile Tilapia Skin (Oreochromis niloticus)

Tozetto,

Santos Rocha,

Assis de Andrade

et al. 2023

Chemistry & Biodiversity

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Oreochromis niloticus (Nile tilapia) skin is a by‐product of Brazilian fish farming, rich in collagen. The present study aims to evaluate the wound healing, antioxidant, and antimicrobial potential of the raw hydrolyzed extract of Nile tilapia skin, as well as the identification of the main compounds. The in vitro activity was performed using antioxidant, antimicrobial and scratch wound healing assays. An in vivo experiment was performed to evaluate the wound healing potential. On days 1, 7, 14 and 21, the lesions were photographed to assess wound retraction and on the 7th, 14th and 21st days the skins were removed for histological evaluation and the blood of the animals was collected for glutamic oxaloacetic transaminase and glutamic pyruvic transaminase determination. The chemical study was carried out through liquid chromatography‐tandem mass spectrometry and de novo sequencing of peptides. The in vitro assays showed a reduction of the gap area in 24 h, dose‐dependent antimicrobial activity for both bacteria, and antioxidant activity. The chemical analysis highlighted the presence of active biopeptides. The histological evaluation showed that the raw hydrolyzed extract of Nile tilapia skin has a healing potential, and does not present toxicological effects; therefore, is promising for the treatment of wounds.

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Tri‐ and dipeptides identification in whey protein and porcine liver protein hydrolysates by fast LC–MS/MS neutral loss screening and de novo sequencing

Cited by 4 publications

References 41 publications

Obtaining of bioactive di‐ and tripeptides from enzymatic hydrolysis of soybean meal and its protein isolate using Alcalase® and Neutrase®

Obtaining of bioactive di‐ and tripeptides from enzymatic hydrolysis of soybean meal and its protein isolate using Alcalase® and Neutrase®

Optimization and Characterization of Protein Extraction from Asparagus Leafy By-Products

Study of the Antioxidant, Antimicrobial, and Wound Healing Properties of Raw Hydrolyzed Extract from Nile Tilapia Skin (Oreochromis niloticus)

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