Simultaneous determination of Angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique.

Simultaneous determination of Angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique. Research Abstract Details 

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Simultaneous determination of Angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique. Abstract Text:

Xiao-Lin Zhu,Toshiro Matsui,Keisuke Watanabe,Koso Shiraishi,Tatsuro Ueki,Kiyoshi Matsumoto,Xiao-Lin Zhu,Toshiro Matsui,Keisuke Watanabe,Koso Shiraishi,Tatsuro Ueki,Kiyoshi Matsumoto,

A replicate heart-cut column-switching HPLC method combined with two switching valves was newly developed for the simultaneous determination of three antihypertensive peptides (Ala-Phe, Tyr-Pro, and Trp-Tyr) in tryptic casein hydrolysate in one run-in assay. After a first separation on an octadecyl silane (ODS) column, heart-cuts of each peptide were individually separated on a subsequent analytical ODS column: 26% acetonitrile for Ala-Phe and Tyr-Pro (32% for Trp-Tyr) in 0.1% trifluoroacetic acid containing 10 mM sodium 1-octanesulfonate at 0.8 mL/min. Ala-Phe, Tyr-Pro, and Trp-Tyr in casein hydrolysate were determined within 70 min to be 0.377 +/- 0.037 mg/g, 2.50 +/- 0.26 mg/g, and 0.096 +/- 0.008 mg/g, respectively.

Simultaneous determination of Angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique. Publishing Authors By Initials

XL Zhu,T Matsui,K Watanabe,K Shiraishi,T Ueki,K Matsumoto,XL Zhu,T Matsui,K Watanabe,K Shiraishi,T Ueki,K Matsumoto,

For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research

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Simultaneous determination of Angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of agricultural and food chemistry

VOLUME: 55

Page Numbers: 8367-71

Journal Abbreviation: J. Agric. Food Chem.

ISSN: 0021-8561

DAY: 10

MONTH: 10

YEAR: 2007

Simultaneous determination of Angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique. Information

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LANGUAGE: eng

NlmUniqueID: 374755

Simultaneous determination of Angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique. Keywords Mesh Terms:

KEYWORDS: Trypsin

MESH TERMS: analysis

Chemical & Substance for Abstract: Simultaneous determination of Angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique. Information

Substance Name: Trypsin

Registry Number: EC 3.4.21.4

Grant and Affiliation Information for Simultaneous determination of Angiotensin I-converting enzyme inhibitory peptides in tryptic casein hydrolysate by high-performance liquid chromatography combined with a replicate heart-cut column-switching technique.

AFFILIATION: Division of Bioscience and Bioenvironmental Sciences, Faculty of Agriculture, Graduate School of Kyushu University, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan.

Country: United States

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MEDLINETA: J Agric Food Chem

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