Applications of NMR Spectroscopy 2016
DOI: 10.2174/9781681082875116050003
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Application of NMR Spectroscopy for Structural Characterization of Bioactive Peptides Derived from Food Protein

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Cited by 5 publications
(6 citation statements)
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“…The presence of numerous peptides with different sequences may also cumulatively affect the ACE inhibitory activity values of various MWCO fractions. These results are in agreement with the results reported in the literature on different protein sources (Kamran, Salampessy, & Reddy, 2016).…”
Section: Resultssupporting
confidence: 93%
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“…The presence of numerous peptides with different sequences may also cumulatively affect the ACE inhibitory activity values of various MWCO fractions. These results are in agreement with the results reported in the literature on different protein sources (Kamran, Salampessy, & Reddy, 2016).…”
Section: Resultssupporting
confidence: 93%
“…Consumption of food protein results in beneficial effects on human health. These proteins are derived from animal and plant sources, for example, milk, eggs, cheese, meat, fish, soy, rice, wheat and legumes (Kamran & Reddy, 2018; Kamran, Salampessy, & Reddy, 2016; Korhonen & Pihlanto, 2006; Pritchard, Phillips, & Kailasapathy, 2010). The beneficial effects of these food proteins are enhanced either by gastrointestinal enzymatic hydrolysis or by microbial fermentation to generate peptides with improved biological activities.…”
Section: Introductionmentioning
confidence: 99%
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“…It is important to determine the primary sequence and the secondary structure of peptides as these structural elements are related to their biological activities. Structural characterization of identified bioactive peptides is usually carried out using the mass spectrometry (MS) technique for amino acid sequencing followed by molecular spectroscopy for secondary structure determination [173][174][175][176]. This review specifically focuses on the structure-activity relationship (SAR) aspects of antimicrobial peptides (AMPs), antihypertensive peptides, and antioxidative peptides (AOPs), given the abundance of literature supporting these prediction models.…”
Section: Structure-activity Relationship (Sar)mentioning
confidence: 99%
“…The secondary structures of natural AMPs are predominantly β-sheets and α-helices [183]. However, the literature on the secondary structures of AMPs derived from food proteins is limited [176]. Therefore, limiting the discussion on the SAR of AMPs to natural peptides.…”
Section: Antimicrobial Peptides (Amps)mentioning
confidence: 99%