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Article Abstract
Lactoferrin is crucial for the mammalian immune system, but the extraction of bovine lactoferrin (bLF) is low, and human lactoferrin in breast milk is costly. Although there are some reports on heterologous expression of lactoferrin, limited knowledge is available. In this study, structural characteristics and antioxidant activity of binary compounds formed by covalent modification of plant derived recombinant human lactoferrin (OsrhLF) with four typical carbohydrates including sodium alginate (SA), maltodextrin (Mal), pectin (Pec), and lactose (Lac). Results indicated that the structure of both bLF and OsrhLF unfolded, with side chain lysine or terminal amino acids forming CN bonds with aldehydes, altering their structure and improving stability and hydrophilicity. Compared with OsrhLF, the thermal denaturation temperatures of H-OsrhLF-Mal and H-OsrhLF-Lac increased by 56.8 °C and 58.4 °C, respectively. OsrhLF exhibited superior surface hydrophilicity and thermal stability compared to bLF, with Mal showing the most significant effect, aiding future functional food applications.
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| http://dx.doi.org/10.1016/j.foodchem.2024.142300 | DOI Listing |
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