| Multiple reaction monitoring-based determination of bovine α-lactalbumin in infant formulas and whey protein concentrates by ultra-high performance liquid chromatography-tandem mass spectrometry using tryptic signature peptides and synthetic peptide standards. | |
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MedLine Citation:
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PMID: 22541822 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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The determination of α-lactalbumin in various dairy products attracts wide attention in multidiscipline fields because of its nutritional and biological functions. In the present study, we quantified the bovine α-lactalbumin in various infant formulas and whey protein concentrates using ultra-high performance liquid chromatography coupled to tandem mass spectrometer in multiple reaction monitoring mode. Bovine α-lactalbumin was quantified by employing the synthetic internal standard based on the molar equivalent relationship among the internal standard, bovine α-lactalbumin and their signature peptides. This study especially focused on the recovery rates of the sample preparation procedure and robust quantification of total bovine α-lactalbumin in its native and thermally denatured form with a synthetic internal standard KILDKVGINNYWLAHKALCSE. The observed recovery rates of bovine α-lactalbumin ranged from 95.8 to 100.6% and the reproducibility was excellent (RSD<6%) at different spiking levels. The limit of quantitation is 10mg/100g for infant formulas and whey protein concentrates. In order to validate the applicability of the method, 21 brands of infant formulas were analyzed. The acquired contents of bovine α-lactalbumin were 0.67-1.84g/100g in these infant formulas in agreement with their label claimed values. The experiment of heat treatment time showed that the loss of native α-lactalbumin enhanced with an increasing intensity of heat treatment. Comparing with Ren's previous method by analysis of only native bovine α-lactalbumin, the present method at the peptide level proved to be highly suitable for measuring bovine α-lactalbumin in infant formulas and whey protein concentrates, avoiding forgoing the thermally induced denatured α-lactalbumin caused by the technological processing. |
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Authors:
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Jingshun Zhang; Shiyun Lai; Yu Zhang; Baifen Huang; Duo Li; Yiping Ren |
Publication Detail:
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Type: Journal Article Date: 2012-03-29 |
Journal Detail:
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Title: Analytica chimica acta Volume: 727 ISSN: 1873-4324 ISO Abbreviation: Anal. Chim. Acta Publication Date: 2012 May |
Date Detail:
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Created Date: 2012-04-30 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370534 Medline TA: Anal Chim Acta Country: Netherlands |
Other Details:
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Languages: eng Pagination: 47-53 Citation Subset: IM |
Copyright Information:
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Copyright © 2012 Elsevier B.V. All rights reserved. |
Affiliation:
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Department of Food Science and Nutrition, College of Biosystems Engineering and Food Science, Zhejiang University, Hangzhou 310058, China; Zhejiang Provincial Center for Disease Prevention and Control, Hangzhou 310051, China. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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