The pH-dependent protection of α-galactosidase activity by proteins against degradative enzymes during soymilk in vitro digestion

Yanyun Cao; Eric M. Xiong; Alma D. True; Youling L. Xiong

doi:10.1016/j.lwt.2016.01.052

The pH-dependent protection of α-galactosidase activity by proteins against degradative enzymes during soymilk in vitro digestion

Yanyun Cao, Eric M. Xiong, Alma D. True, Youling L. Xiong

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

α-Galactosidase (α-GAL) dietary supplement is used to alleviate flatulence discomfort caused by raffinose family oligosaccharides (RFOs), but reported efficacy varies among consumers. This study investigated the hypothesis that factors such as stomach acid, gastrointestinal (GI) enzymes (pepsin and pancreatin), and food proteins could affect the activity of α-GAL against RFOs. Strong acidic conditions (pH < 2.0) and GI proteases were found detrimental to α-GAL whereas soy protein could protect α-GAL. In soymilk samples with 1 and 5 mg/mL protein, α-GAL retained 60 and 100% of activity (P < 0.05) throughout the entire digestion (pepsin + pancreatin, 3 h) at pH 2.5 whereas α-GAL was completely inactivated within 1 h of pepsin digestion in water. Isolated soy protein was more protective of α-GAL than soymilk protein. The results were corroborated by SDS-PAGE and the release of galactose as evidenced with the thin layer chromatography.

Original language	English
Pages (from-to)	244-250
Number of pages	7
Journal	LWT - Food Science and Technology
Volume	69
DOIs	https://doi.org/10.1016/j.lwt.2016.01.052
State	Published - Jun 1 2016

Bibliographical note

Funding Information:
This is publication No. 15-07-118 of the Kentucky Agricultural Experiment Station and is published with the approval of the Director. This work is supported by the National Institute of Food and Agriculture , U.S. Department of Agriculture , Hatch project number 1005724.

Publisher Copyright:
© 2016 Elsevier Ltd.

Keywords

Digestive enzymes
Raffinose
Soy protein
pH
α-Galactosidase

ASJC Scopus subject areas

Food Science

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10.1016/j.lwt.2016.01.052

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title = "The pH-dependent protection of α-galactosidase activity by proteins against degradative enzymes during soymilk in vitro digestion",

abstract = "α-Galactosidase (α-GAL) dietary supplement is used to alleviate flatulence discomfort caused by raffinose family oligosaccharides (RFOs), but reported efficacy varies among consumers. This study investigated the hypothesis that factors such as stomach acid, gastrointestinal (GI) enzymes (pepsin and pancreatin), and food proteins could affect the activity of α-GAL against RFOs. Strong acidic conditions (pH < 2.0) and GI proteases were found detrimental to α-GAL whereas soy protein could protect α-GAL. In soymilk samples with 1 and 5 mg/mL protein, α-GAL retained 60 and 100% of activity (P < 0.05) throughout the entire digestion (pepsin + pancreatin, 3 h) at pH 2.5 whereas α-GAL was completely inactivated within 1 h of pepsin digestion in water. Isolated soy protein was more protective of α-GAL than soymilk protein. The results were corroborated by SDS-PAGE and the release of galactose as evidenced with the thin layer chromatography.",

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note = "Funding Information: This is publication No. 15-07-118 of the Kentucky Agricultural Experiment Station and is published with the approval of the Director. This work is supported by the National Institute of Food and Agriculture , U.S. Department of Agriculture , Hatch project number 1005724. Publisher Copyright: {\textcopyright} 2016 Elsevier Ltd.",

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AU - True, Alma D.

AU - Xiong, Youling L.

N1 - Funding Information: This is publication No. 15-07-118 of the Kentucky Agricultural Experiment Station and is published with the approval of the Director. This work is supported by the National Institute of Food and Agriculture , U.S. Department of Agriculture , Hatch project number 1005724. Publisher Copyright: © 2016 Elsevier Ltd.

PY - 2016/6/1

Y1 - 2016/6/1

N2 - α-Galactosidase (α-GAL) dietary supplement is used to alleviate flatulence discomfort caused by raffinose family oligosaccharides (RFOs), but reported efficacy varies among consumers. This study investigated the hypothesis that factors such as stomach acid, gastrointestinal (GI) enzymes (pepsin and pancreatin), and food proteins could affect the activity of α-GAL against RFOs. Strong acidic conditions (pH < 2.0) and GI proteases were found detrimental to α-GAL whereas soy protein could protect α-GAL. In soymilk samples with 1 and 5 mg/mL protein, α-GAL retained 60 and 100% of activity (P < 0.05) throughout the entire digestion (pepsin + pancreatin, 3 h) at pH 2.5 whereas α-GAL was completely inactivated within 1 h of pepsin digestion in water. Isolated soy protein was more protective of α-GAL than soymilk protein. The results were corroborated by SDS-PAGE and the release of galactose as evidenced with the thin layer chromatography.

AB - α-Galactosidase (α-GAL) dietary supplement is used to alleviate flatulence discomfort caused by raffinose family oligosaccharides (RFOs), but reported efficacy varies among consumers. This study investigated the hypothesis that factors such as stomach acid, gastrointestinal (GI) enzymes (pepsin and pancreatin), and food proteins could affect the activity of α-GAL against RFOs. Strong acidic conditions (pH < 2.0) and GI proteases were found detrimental to α-GAL whereas soy protein could protect α-GAL. In soymilk samples with 1 and 5 mg/mL protein, α-GAL retained 60 and 100% of activity (P < 0.05) throughout the entire digestion (pepsin + pancreatin, 3 h) at pH 2.5 whereas α-GAL was completely inactivated within 1 h of pepsin digestion in water. Isolated soy protein was more protective of α-GAL than soymilk protein. The results were corroborated by SDS-PAGE and the release of galactose as evidenced with the thin layer chromatography.

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The pH-dependent protection of α-galactosidase activity by proteins against degradative enzymes during soymilk in vitro digestion

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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