| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 34934 | Process Biochemistry | 2012 | 8 Pages |
The production of glycated lysozyme (LZM), with galactose, galactooligosaccharides (GOSs) and potato galactan through the Maillard reaction, was investigated. The percent blocked lysine, estimated from the furosine content, reached a maximum value of 11.2% for LZM:galactan conjugates after 1 day incubation at a aw of 0.65. A maximum percent blocked lysine of 7.0 and 13.5% were obtained for LZM:galactose/GOS conjugates at a lower aw of 0.45 after 3 and 7 days, respectively. However, the low percent blocked lysine and the high protein aggregation index of LZM:galactose/GOS conjugates at aw 0.79 and 0.65 revealed the prevalence of the degradation of the Amadori compounds and the protein cross-linking. Mass spectrometry of LZM conjugates revealed the formation of different glycoforms. Glycated LZMs containing up to seven galactose moieties were formed; while only mono- and diglycated LZMs with GOSs were detected. 2–3 mol of galactan were conjugated to 1 mol of LZM. Response surface methodology, based on a 5-level and 3-factor central composite design, revealed that molar ratio and temperature were the most significant variables for the glycation of LZM with GOSs. The optimal conditions leading to a high percent blocked lysine (16.11%) with a low protein aggregation index (0.11) were identified: temperature of 49.5 °C, LZM:GOS molar ratio of 1:9 and aw of 0.65. To the best of our knowledge, this is the first study on the optimization of LZM glycation with GOSs.
► Maillard reaction is a potential strategy to synthesize new glycated proteins. ► Conjugation of GOSs to LZM might increase the persistence of their prebiotic activity. ► Galactose showed a high reactivity resulting in the formation of multiglycated LZM. ► Limited interactions of GOS/galactan to LZM led to narrow distribution of glycoform. ► Our study is the first investigating interactions between Maillard reaction parameters.
