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Enzymatic hydrolysis of whey protein concentrates: Peptide HPLC profiles

Title
Enzymatic hydrolysis of whey protein concentrates: Peptide HPLC profiles
Type
Article in International Scientific Journal
Year
2004
Authors
M. V. T. Mota
(Author)
Other
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Isabel Ferreira
(Author)
FFUP
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Maria Beatriz Oliveira
(Author)
FFUP
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C. Rocha
(Author)
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Maria do Pilar Gonçalves
(Author)
FEUP
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Journal
Vol. 27 No. 16
Pages: 2625-2639
ISSN: 1082-6076
Publisher: Taylor & Francis
Indexing
Publicação em ISI Web of Science ISI Web of Science
COMPENDEX
Scientific classification
FOS: Natural sciences > Chemical sciences
Other information
Authenticus ID: P-000-D2P
Abstract (EN): Hydrolysis of whey protein concentrates (WPCs) at different temperatures and pHs, using three enzymes: pepsin, trypsin, and Alcalase(R), was monitored during more than 5 hr by reversed phase HPLC/UV, using a column containing a polystyrene-divinylbenzene copolymer-based packing, and an elution gradient from 8% to 80% acetonitrile containing 0.1% TFA. Peptides were separated according to their polarity and size, and degradation of alpha-lactalbumin (alpha-la) and beta-lactoglobulin (beta-lg) was evaluated. The three proteolytic enzymes (pepsin, trypsin, and Alcalase(R)) employed for hydrolysis of WPCs led to different kinetics of degradation of beta-lg. alpha-la degradation after 15 min was almost complete for the three enzymes. The hydrolysis catalysed by each enzyme resulted in different peptide profiles by HPLC/UV. Hydrolysates produced by pepsin (HP) were resolved into three main fractions of high retention times, while tripsin hydrolysates (HT) were resolved into nine major peaks and Alcalase(R) hydrolysates (HA) were resolved into 12 major peaks, presenting a wide range of polarities and sizes. Although, with different beta-lg hydrolysis extension, chromatographic profiles of the degradation and formation of peptides can be used as a finger print of the type of enzyme used, because peptide profile is not affected either by temperature or pH.
Language: English
Type (Professor's evaluation): Scientific
No. of pages: 15
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