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Sammanfattning

Denaturation temperatures (T(max)) of folate binding protein (FBP) complexed with various folate derivatives were studied using differential scanning calorimetry. Surface plasmon resonance technique was used to elucidate the effect of heat treatment, i.e., pasteurization and UHT treatment, of FBP on FBP content and its binding capacity to folate. The folate derivatives studied were (6S)5-HCO-H(4)folate, (6S)5-CH(3)-H(4)folate and pteroy-L-glutamic acid (PteGlu). The results showed that different folate forms affected the heat denaturation temperature of FBP differently. Apo-FBP underwent an endothermic transition with a maximum at 60.5 +/- 0 degrees C. After ligand binding, the maximum of the denaturation shifted with a transition maximum at 72.4 +/- 0.3 degrees C for (6S)5-HCO-H(4)folate and 78.7 +/- 0.5 degrees C for (6S)5-CH(3)-H(4)folate. The highest temperature shift was observed for PteGlu with maximum transition temperature at 83.7 +/- 0.2 degrees C. Pasteurization temperatures did not eliminate the binding capacity of FBP regardless of folate form bound, whereas the UHT-treatment did. (c) 2009 Elsevier Ltd. All rights reserved.

Publicerad i

International Dairy Journal
2009, volym: 19, nummer: 8, sidor: 437-442
Utgivare: ELSEVIER SCI LTD

SLU författare

UKÄ forskningsämne

Livsmedelsvetenskap

Publikationens identifierare

  • DOI: https://doi.org/10.1016/j.idairyj.2009.01.004

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/61350