Journal
FOOD HYDROCOLLOIDS
Volume 74, Issue -, Pages 267-274Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2017.08.016
Keywords
Microencapsulating; Globular proteins; Coacervation; Differential scanning; Calorimetry; Electrostatic interaction
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Funding
- CNPq [310861/2015-2]
- FAPERJ [E26/201.486/2014]
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The formation of a heteroprotein complex obtained by the interaction of bovine serum albumin (BSA) and lysozyme (Lys) was investigated by pH variation using turbidimetric analysis and zeta potential (z) at different protein ratios and NaCl concentrations. The complexes were formed in a pH range between 8.0 and 11.0, with the ratio r = 0.5 at pH 9.0 presenting the highest complexation. The addition of NaCl decreased the interaction at concentrations of 10 mM. The complex formation occurred between the isoelectric points (pI) of the proteins, close to a balance of charges, mainly by electrostatic interactions with some participation of hydrogen bonds. Differential scanning calorimetry suggested that the interaction gave rise to a new biopolymer due to the formation of a single denaturation point at 67 degrees C. The structures formed had an average size of similar to 1.7 mm, well above that of the isolated proteins, and microscopic analysis revealed that the complexes had a globular structure. BSA/Lys complexes may be a potential bioactive encapsulating agent and may be used as a food ingredient. (C) 2017 Elsevier Ltd. All rights reserved.
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