Conformational changes in bovine lactoferrin induced by slow or fast temperature increases
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Waleska D. Schwarcz
Abstract
Lactoferrin (LF) is an iron-binding protein present in several secreted substances, such as milk, and has broad antimicrobial and physiological properties. Because high temperatures may affect protein stability and its functional properties, we investigated the effect of heat on bovine LF structure and stability. The effects of temperatures used during the pasteurization process on LF and its relationship to protein functionality were studied. Conformational changes were monitored using spectroscopic techniques, such as circular dichroism (CD) and fluorescence spectroscopy. The CD data at 70°C showed that LF's secondary structure is drastically and irreversibly affected when the temperature is gradually increased. The same effect is observed when the temperature is gradually raised from 25°C to 105°C and changes are monitored by tryptophan fluorescence emission. We also verified the effects of simulating the pasteurization process; LF remained well structured during the entire process and this result was not time-dependent. Owing to preservation of the secondary structure with changes in the tertiary structure, we thus believe that pasteurization might cause LF to change into an intermediate partially folded state. A better understanding of heat stability is important for the use of LF as a bioactive component in food.
©2008 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Editors' Note
- Editors' Note
- Editorial
- Farewell to Hans Fritz, Executive Editor
- Guest Editorial
- Highlight on Advances in Proteolysis Research
- Highlight: 5th General Meeting of the International Proteolysis Society 2007
- Proteinases as hormones: targets and mechanisms for proteolytic signaling
- Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution
- Alternative pathways for production of β-amyloid peptides of Alzheimer's disease
- Bauhinia Kunitz-type proteinase inhibitors: structural characteristics and biological properties
- Angiotensin-converting enzyme limits inflammation elicited by Trypanosoma cruzi cysteine proteases: a peripheral mechanism regulating adaptive immunity via the innate kinin pathway
- How Na+ activates thrombin – a review of the functional and structural data
- Cancer cells, adipocytes and matrix metalloproteinase 11: a vicious tumor progression cycle
- Isoaspartate residues dramatically influence substrate recognition and turnover by proteases
- Isoaspartate-containing amyloid precursor protein-derived peptides alter efficacy and specificity of potential β-secretases
- Trial of the cysteine cathepsin inhibitor JPM-OEt on early and advanced mammary cancer stages in the MMTV-PyMT-transgenic mouse model
- Metastasis-associated C4.4A, a GPI-anchored protein cleaved by ADAM10 and ADAM17
- Intestine-specific expression of green fluorescent protein-tagged cathepsin B: proof-of-principle experiments
- Substrate specificity determination of mouse implantation serine proteinase and human kallikrein-related peptidase 6 by phage display
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- Protein Structure and Function
- Contribution of the C30/C75 disulfide bond to the biological properties of onconase
- Conformational changes in bovine lactoferrin induced by slow or fast temperature increases
