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Effects of genetic ...
Effects of genetic variants and sialylation on in vitro digestibility of purified κ-casein
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- Sheng, Bulei (författare)
- Aarhus University
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- Nielsen, Søren D. (författare)
- Aarhus University
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- Glantz, Maria (författare)
- Lund University,Lunds universitet,Avdelningen för livsmedel och läkemedel,Institutionen för processteknik och tillämpad biovetenskap,Institutioner vid LTH,Lunds Tekniska Högskola,Division of Food and Pharma,Department of Process and Life Science Engineering,Departments at LTH,Faculty of Engineering, LTH
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- Paulsson, Marie (författare)
- Lund University,Lunds universitet,Avdelningen för livsmedel och läkemedel,Institutionen för processteknik och tillämpad biovetenskap,Institutioner vid LTH,Lunds Tekniska Högskola,Division of Food and Pharma,Department of Process and Life Science Engineering,Departments at LTH,Faculty of Engineering, LTH
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- Poulsen, Nina A. (författare)
- Aarhus University
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- Larsen, Lotte B. (författare)
- Aarhus University
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(creator_code:org_t)
- American Dairy Science Association, 2022
- 2022
- Engelska 12 s.
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Ingår i: Journal of Dairy Science. - : American Dairy Science Association. - 0022-0302. ; 105:4, s. 2803-2814
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Abstract
Ämnesord
Stäng
- Milk with different κ-casein (CN) phenotypes has previously been found to influence its gastric digestion rate. Therefore, the aim of the present study is to disentangle contributions of genetic variation and its related sialylation on the in vitro digestion process of κ-CN. Accordingly, κ-CN was purified from milk representing homozygous cows with κ-CN phenotypes AA, BB, or EE and used as substrate molecules in model studies using the INFOGEST 2.0 in vitro static digestion model. Furthermore, the effect of removal of the terminal sialic acids present on the O-linked oligosaccharides of the purified κ-CN A, B, and E protein variants were studied by desialylation enzymatic assays. The κ-CN proteins were purified by reducing anion exchange chromatography with purities of variants A, B, and E of 93.0, 97.1, and 90.0%, respectively. Protein degradations of native and desialylated κ-CN isolates in gastric and intestinal phases were investigated by sodium dodecyl sulfate-PAGE, degree of hydrolysis (DH), and liquid chromatography electrospray ionization mass spectrometry. It was shown that after purification, the κ-CN molecules reassembled into multimer states, which then constituted the basis for the digestion studies. As assessed by DH, purified variants A and E were found to exhibit faster in vitro digestion rates in both gastric and intestinal phases compared with variant B. Desialylation increased both gastric and intestinal digestion rates for all variants, as measured by DH. In the gastric phase, desialylation promoted digestion of variant B at a rate comparable with native variants A and E, whereas in the intestinal phase, desialylation of variant B promoted better digestion than native A or E. Taken together, the results confirm that low glycosylation degree of purified κ-CN promotes faster in vitro digestion rates, and that desialylation of the O-linked oligosaccharides further promotes digestion. This finding could be applied to produce dairy products with enhanced digestibility.
Ämnesord
- TEKNIK OCH TEKNOLOGIER -- Annan teknik -- Livsmedelsteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Other Engineering and Technologies -- Food Engineering (hsv//eng)
Nyckelord
- degree of hydrolysis
- digestion rate
- glycosylation
- sialic acid
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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