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

Author(s):  
Camila B. Poliseli ◽  
Angelica P.P. Tonin ◽  
Fernanda C. Martinez ◽  
Nicholas C. Nascimento ◽  
Vilmar Braz Junior ◽  
...  
2020 ◽  
Vol 10 (7) ◽  
pp. 2290 ◽  
Author(s):  
Paula Borrajo ◽  
Mirian Pateiro ◽  
Mohammed Gagaoua ◽  
Daniel Franco ◽  
Wangang Zhang ◽  
...  

In order to make the by-products generated from the porcine industry more valuable, pig livers were used in this trial to obtain protein hydrolysates. Three proteases (alcalase, bromelain, and papain) were utilized for enzymatic hydrolysis with two different durations, 4 and 8 hours. Ultrafiltration process was used for the recovery of the extracts, employing three different membrane pore sizes (30, 10, and 5 kDa). The porcine livers contained considerable amounts of protein (19.0%), considering they are almost composed of water (74.1%). The antioxidant activity of the obtained hydrolysates was investigated using four antioxidant methods (2,2-Diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, 2-2′-Azino-di-[3-ethylbenzthiazoline sulfonate] (ABTS) radical scavenging activity, ferric reducing antioxidant power assay (FRAP), and oxygen radical absorbance capacity assay (ORAC)). Antibacterial properties were also measured against Gram-negative and Gram-positive bacteria. Results indicated that the three studied factors (type of enzyme, membrane pore size, and time) significantly affected the parameters evaluated. Hydrolysates obtained at 8 hours with alcalase had the best antioxidant properties. The 30 kDa alcalase extracts exhibited the highest DPPH (562 µg Trolox/g), FRAP (82.9 µmol Fe2+/100 g), and ORAC (53.2 mg Trolox/g) activities, while for ABTS the 10 kDa alcalase showed the higher values (1068 mg ascorbic acid/100 g). Concerning the antibacterial activity, 30 kDa hydrolysates obtained with bromelain for 4 hours exhibited the highest antimicrobial capacity, providing an inhibition of 91.7%.


2021 ◽  
Vol 6 (7) ◽  
pp. 1826-1828
Author(s):  
Ping Jiang ◽  
Guangpei Xu ◽  
Yanfei He ◽  
Taotao Sun ◽  
Changli Liu ◽  
...  

Author(s):  
Mathieu Dupré ◽  
Magalie Duchateau ◽  
Rebecca Sternke-Hoffmann ◽  
Amelie Boquoi ◽  
Christian Malosse ◽  
...  

2018 ◽  
Vol 89 (9) ◽  
pp. 1348-1354 ◽  
Author(s):  
Hajime Nakada ◽  
Motoko Ohata ◽  
Mari Hosaka ◽  
Hiroshi Ochi ◽  
Fumiaki Abe ◽  
...  

2008 ◽  
Vol 06 (03) ◽  
pp. 467-492 ◽  
Author(s):  
KANG NING ◽  
NAN YE ◽  
HON WAI LEONG

Peptide sequencing plays a fundamental role in proteomics. Tandem mass spectrometry, being sensitive and efficient, is one of the most commonly used techniques in peptide sequencing. Many computational models and algorithms have been developed for peptide sequencing using tandem mass spectrometry. In this paper, we investigate general issues in de novo sequencing, and present results that can be used to improve current de novo sequencing algorithms. We propose a general preprocessing scheme that performs binning, pseudo-peak introduction, and noise removal, and present theoretical and experimental analyses on each of the components. Then, we study the antisymmetry problem and current assumptions related to it, and propose a more realistic way to handle the antisymmetry problem based on analysis of some datasets. We integrate our findings on preprocessing and the antisymmetry problem with some current models for peptide sequencing. Experimental results show that our findings help to improve accuracies for de novo sequencing.


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