Multi-step thermally induced transitions of beta-lactoglobulin - An in situ spectroscopy approach

• Type: Article in International Scientific Journal
• Date: 2020

Authors

Rodrigues, RM (Author) Other; Claro, B (Author) Other; Bastos, M (Author) FCUP; Pereira, RN (Author) Other; Vicente, AA (Author) FCUP; Petersen, SB (Author) Other

Journal

Title: International Dairy Journal

Vol. 100

ISSN: 0958-6946

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 5 Citations

Scopus - 6 Citations

Other information

Authenticus ID: P-00R-4C3

DOI: 10.1016/j.idairyj.2019.104562

Abstract (EN): An in-situ approach based in multiple spectroscopic techniques and benchmarked with DSC was used to characterise beta-Lg thermally-induced transitions. The methodology applied overcomes previously reported limitations by ensuring similar experimental conditions in different determinations, non-aggregation conditions and allowing differentiation between fluorescent variations due to collisional quenching and structural modifications. These experimental improvements along with the correlation of complementary data from the assessment of several unfolding-related events, allowed a real time, precise and detailed description of the unfolding/refolding pathways of beta-Lg. The existence of a complex multi-step unfolding mechanism was confirmed, with a focus on the reversible conformational changes. The elusive unfolding intermediates were characterised in terms of structural swelling, hydrophobic sites accessibility and tryptophan exposure. This approach allowed establishing a clear order of events during thermally-induced structural changes, representing a step forward in the understanding of protein stability and interactions, useful, e.g., when establishing heat treatments of dairy products.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 8