Enzyme catalysed production of sialylated human milk oligosaccharides and galactooligosaccharides by Trypanosoma cruzi trans-sialidase

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Enzyme catalysed production of sialylated human milk oligosaccharides and galactooligosaccharides by Trypanosoma cruzi trans-sialidase. / Holck, Jesper; Larsen, Dorte M.; Michalak, Malwina; Li, Haiying; Kjærulff, Louise; Kirpekar, Finn; Gotfredsen, Charlotte H.; Forssten, Sofia; Ouwehand, Arthur C.; Mikkelsen, Jørn D.; Meyer, Anne S.

In: New Biotechnology, Vol. 31, No. 2, 2014, p. 156-165.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Holck, J, Larsen, DM, Michalak, M, Li, H, Kjærulff, L, Kirpekar, F, Gotfredsen, CH, Forssten, S, Ouwehand, AC, Mikkelsen, JD & Meyer, AS 2014, 'Enzyme catalysed production of sialylated human milk oligosaccharides and galactooligosaccharides by Trypanosoma cruzi trans-sialidase', New Biotechnology, vol. 31, no. 2, pp. 156-165. https://doi.org/10.1016/j.nbt.2013.11.006

APA

Holck, J., Larsen, D. M., Michalak, M., Li, H., Kjærulff, L., Kirpekar, F., Gotfredsen, C. H., Forssten, S., Ouwehand, A. C., Mikkelsen, J. D., & Meyer, A. S. (2014). Enzyme catalysed production of sialylated human milk oligosaccharides and galactooligosaccharides by Trypanosoma cruzi trans-sialidase. New Biotechnology, 31(2), 156-165. https://doi.org/10.1016/j.nbt.2013.11.006

Vancouver

Holck J, Larsen DM, Michalak M, Li H, Kjærulff L, Kirpekar F et al. Enzyme catalysed production of sialylated human milk oligosaccharides and galactooligosaccharides by Trypanosoma cruzi trans-sialidase. New Biotechnology. 2014;31(2):156-165. https://doi.org/10.1016/j.nbt.2013.11.006

Author

Holck, Jesper ; Larsen, Dorte M. ; Michalak, Malwina ; Li, Haiying ; Kjærulff, Louise ; Kirpekar, Finn ; Gotfredsen, Charlotte H. ; Forssten, Sofia ; Ouwehand, Arthur C. ; Mikkelsen, Jørn D. ; Meyer, Anne S. / Enzyme catalysed production of sialylated human milk oligosaccharides and galactooligosaccharides by Trypanosoma cruzi trans-sialidase. In: New Biotechnology. 2014 ; Vol. 31, No. 2. pp. 156-165.

Bibtex

@article{b8997e4c51ae47e3ace08809e16841f2,
title = "Enzyme catalysed production of sialylated human milk oligosaccharides and galactooligosaccharides by Trypanosoma cruzi trans-sialidase",
abstract = "A Trypanosoma cruzi trans-sialidase (E.C. 3.2.1.18) was cloned into Pichia pastoris and expressed. The pH and temperature optimum of the enzyme was determined as pH 5.7 and 30°C. Using casein glycomacropeptide (CGMP) and lactose as sialyl-donor and acceptor respectively, the optimal donor/acceptor ratio for the trans-sialidase catalysed 3'-sialyllactose production was found to be 1:4. Quantitative amounts of 3'-sialyllactose were produced from CGMP and lactose at a yield of 40. mg/g CGMP. The 3'-sialyllactose obtained exerted a stimulatory effect on selected probiotic strains, including different Bifidobacterium strains in single culture fermentations. The trans-sialidase also catalysed the transfer of sialic acid from CGMP to galacto-oligosaccharides (GOS) and to the human milk oligosaccharide (HMO) backbone lacto-N-tetraose (LNT) to produce 3'-sialyl-GOS, including doubly sialylated GOS products, and 3'-sialyl-LNT, respectively. This work thus provides proof of the concept of producing 3'-sialyllactose and potentially other sialylated HMOs as well as sialylated GOS enzymatically by trans-sialidase activity, while at the same time providing valorisation of CGMP, a co-processing product from cheese manufacture.",
author = "Jesper Holck and Larsen, {Dorte M.} and Malwina Michalak and Haiying Li and Louise Kj{\ae}rulff and Finn Kirpekar and Gotfredsen, {Charlotte H.} and Sofia Forssten and Ouwehand, {Arthur C.} and Mikkelsen, {J{\o}rn D.} and Meyer, {Anne S.}",
year = "2014",
doi = "10.1016/j.nbt.2013.11.006",
language = "English",
volume = "31",
pages = "156--165",
journal = "New Biotechnology",
issn = "1871-6784",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Enzyme catalysed production of sialylated human milk oligosaccharides and galactooligosaccharides by Trypanosoma cruzi trans-sialidase

AU - Holck, Jesper

AU - Larsen, Dorte M.

AU - Michalak, Malwina

AU - Li, Haiying

AU - Kjærulff, Louise

AU - Kirpekar, Finn

AU - Gotfredsen, Charlotte H.

AU - Forssten, Sofia

AU - Ouwehand, Arthur C.

AU - Mikkelsen, Jørn D.

AU - Meyer, Anne S.

PY - 2014

Y1 - 2014

N2 - A Trypanosoma cruzi trans-sialidase (E.C. 3.2.1.18) was cloned into Pichia pastoris and expressed. The pH and temperature optimum of the enzyme was determined as pH 5.7 and 30°C. Using casein glycomacropeptide (CGMP) and lactose as sialyl-donor and acceptor respectively, the optimal donor/acceptor ratio for the trans-sialidase catalysed 3'-sialyllactose production was found to be 1:4. Quantitative amounts of 3'-sialyllactose were produced from CGMP and lactose at a yield of 40. mg/g CGMP. The 3'-sialyllactose obtained exerted a stimulatory effect on selected probiotic strains, including different Bifidobacterium strains in single culture fermentations. The trans-sialidase also catalysed the transfer of sialic acid from CGMP to galacto-oligosaccharides (GOS) and to the human milk oligosaccharide (HMO) backbone lacto-N-tetraose (LNT) to produce 3'-sialyl-GOS, including doubly sialylated GOS products, and 3'-sialyl-LNT, respectively. This work thus provides proof of the concept of producing 3'-sialyllactose and potentially other sialylated HMOs as well as sialylated GOS enzymatically by trans-sialidase activity, while at the same time providing valorisation of CGMP, a co-processing product from cheese manufacture.

AB - A Trypanosoma cruzi trans-sialidase (E.C. 3.2.1.18) was cloned into Pichia pastoris and expressed. The pH and temperature optimum of the enzyme was determined as pH 5.7 and 30°C. Using casein glycomacropeptide (CGMP) and lactose as sialyl-donor and acceptor respectively, the optimal donor/acceptor ratio for the trans-sialidase catalysed 3'-sialyllactose production was found to be 1:4. Quantitative amounts of 3'-sialyllactose were produced from CGMP and lactose at a yield of 40. mg/g CGMP. The 3'-sialyllactose obtained exerted a stimulatory effect on selected probiotic strains, including different Bifidobacterium strains in single culture fermentations. The trans-sialidase also catalysed the transfer of sialic acid from CGMP to galacto-oligosaccharides (GOS) and to the human milk oligosaccharide (HMO) backbone lacto-N-tetraose (LNT) to produce 3'-sialyl-GOS, including doubly sialylated GOS products, and 3'-sialyl-LNT, respectively. This work thus provides proof of the concept of producing 3'-sialyllactose and potentially other sialylated HMOs as well as sialylated GOS enzymatically by trans-sialidase activity, while at the same time providing valorisation of CGMP, a co-processing product from cheese manufacture.

U2 - 10.1016/j.nbt.2013.11.006

DO - 10.1016/j.nbt.2013.11.006

M3 - Journal article

C2 - 24316323

AN - SCOPUS:84893741493

VL - 31

SP - 156

EP - 165

JO - New Biotechnology

JF - New Biotechnology

SN - 1871-6784

IS - 2

ER -

ID: 192043793