Isolation of κ-casein glycomacropeptide from bovine whey fraction using food grade anion exchange resin and chitin as an adsorbent

Nakano, T.; Betti, Mirko

doi:10.1017/s0022029919000918

Cited by 11 publications

(18 citation statements)

References 20 publications

(35 reference statements)

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“…Recently, the same group developed a food-grade anion-exchange resin to isolate GMP from the soluble whey fraction. 72 The production of GMP included a 78% recovery of sialic acids, with few contaminating amino acids.…”

Section: Separation and Purification Technologies Of Milk Bioactivesmentioning

confidence: 99%

Bioactives in bovine milk: chemistry, technology, and applications

et al. 2021

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The significance of dairy in human health and nutrition is gaining significant momentum as consumers continue to desire wholesome, nutritious foods to fulfill their health and wellness needs. Bovine milk not only consists of all the essential nutrients required for growth and development, it also provides a broad range of bioactive components that play an important role in managing human homeostasis and immune function. In recent years, milk bioactives, including α-lactalbumin, lactoferrin, glycomacropeptide, milk fat globule membrane, and milk oligosaccharides, have been intensively studied because of their unique bioactivity and functionality. Challenges for the application of these bioactive components in food and pharmaceutical formulations are associated with their isolation and purification on an industrial scale and also with their physical and chemical instability during processing, storage, and digestion. These challenges can be overcome by advanced separation techniques and sophisticated nano- or micro-encapsulation technologies. Current knowledge about the chemistry, separation, and encapsulation technology of major bioactives derived from bovine milk and their application in the food industry is reviewed here.

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Section: Separation and Purification Technologies Of Milk Bioactivesmentioning

confidence: 99%

Bioactives in bovine milk: chemistry, technology, and applications

et al. 2021

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“…It appears that the method can be scaled up without difficulty. a GMP purified by chromatography on chitin column (Nakano and Betti, 2020). b Amino acid composition of genetic variant A (V A ) or variant B (V B ) is based on its primary structure (Eigel et al, 1984).…”

Section: Separation Of Gmp From Swf With Batch Anion Exchange Methods...mentioning

confidence: 99%

Use of batch anion exchange technique for separation of κ-casein glycomacropeptide from bovine whey fraction

Nakano

Betti

2022

Journal of Dairy Research

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Bovine κ-casein glycomacropeptide (GMP) is a sialic acid containing glycopeptide, which is considered as a health promoting compound found in cheese whey. The study described in this research communication was undertaken to determine whether GMP with undetectable level of contaminating protein or phenylalanine can be isolated from bovine whey fraction using batch anion exchange technique with chitin as an adsorbent. A soluble whey fraction (SWF) prepared from 1 g whey protein isolate (WPI) was mixed with a slurry of 1 g chitin, and the mixture was incubated at pH 3.0. After incubation, the mixture was filtered, and the residue obtained (containing chitin-GMP complex) was washed with water and eluted stepwise with 0.5 M NaCl and 2.0 M NaCl. Most of GMP (corresponding to 75.8% of total sialic acid recovered) was eluted with 0.5 M NaCl. The recovered GMP accounted for 5.4% dry weight of WPI (or 18.9% dry weight of SWF). Amino acid analysis showed that there was no detectable level of contaminating amino acids including phenylalanine, histidine, arginine and tyrosine in the GMP fraction. It was concluded that the batch anion exchange method with chitin developed in this study can be used for the isolation of high purity GMP from bovine SWF.

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“…A sample of GMP was a product prepared in our previous study using anion exchange chromatography on Diaion HPA75 (Mitsubishi Chemicals, Tokyo, Japan) (Nakano and Betti, 2020). Its sialic acid content and amino acid composition are given in Table 1.…”

Section: Methodsmentioning

confidence: 99%

“…The content of phosphorus was determined by the malachite green dye binding method (Van Veldhoven and Mannaerts, 1987). Amino acid analysis was carried out on samples hydrolyzed with glass distilled 6 M HCl in the presence of nitrogen gas at 110°C for 24 h as previously described (Nakano and Betti, 2020). Cysteine, methionine and tryptophan were not analyzed.…”

Section: Methodsmentioning

confidence: 99%

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Production of sialic acid rich glycopeptide from bovine κ-casein glycomacropeptide by hydrolyzing with papain

Nakano

Betti

2020

Journal of Dairy Research

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Bovine κ-casein glycomacropeptide (GMP) is a sialic acid containing glycopeptide having many biological activities. The study described in this research communication was undertaken to determine whether sialic acid rich glycopeptide can be produced from GMP by proteinase treatment. A sample of GMP was hydrolyzed with papain, and the obtained hydrolysate was chromatographed on a column of diethylaminoethyl-Sephacel to obtain a glycopeptide fraction (GPF). This product accounted for average 48.1% dry weight of GMP or 81.1% total recovered sialic acid from GMP. The content of sialic acid (expressed as % dry weight) was 1.7 times higher in GPF (22.6) than in unhydrolyzed GMP (13.4). Major differences in amino acid composition between GPF and GMP were found in the contents (mol%) of: lysine (<1 and 4.5, respectively), serine (20.3 and 10.3, approximately twice higher in GPF), asparagine/aspartic acid and isoleucine. The contents of the last two amino acids were approximately twice lower in GPF. On gel filtration chromatography with Sephacryl S-100, GMP was eluted as a single peak with elution volume similar to that of dimeric β-lactoglobulin (36.6 kDa) whereas GPF was eluted in two peaks both with elution volumes greater than that of α-lactalbumin (14.2 kDa). These peak fractions containing high (fraction I) and low (fraction II) molecular size glycopeptides gave different sialic acid to peptide ratio, which was 1.7 times higher in fraction I than in fraction II. Results of size exclusion HPLC on Superdex-75 were consistent with those of gel filtlation chromatography. On cellulose acetate electrophoresis, the mobility of GPF relative to that of GMP as 1.0 was found to average 1.2, suggesting a higher negative charge density in GPF than in GMP. It was concluded that papain digestion of GMP is an efficient method to produce glycopeptide with high sialic acid content.

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Isolation of κ-casein glycomacropeptide from bovine whey fraction using food grade anion exchange resin and chitin as an adsorbent

Cited by 11 publications

References 20 publications

Bioactives in bovine milk: chemistry, technology, and applications

Bioactives in bovine milk: chemistry, technology, and applications

Use of batch anion exchange technique for separation of κ-casein glycomacropeptide from bovine whey fraction

Production of sialic acid rich glycopeptide from bovine κ-casein glycomacropeptide by hydrolyzing with papain

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