Pulsed light improves digestibility of milk allergy lactose protein BLG: Study
Researchers from the University of Granada and Azti-Tecnalia "artificially modified" BLG by degrading its structure using pulsed light treatment - technology typically used to inactivate bacteria in food.
As detailed in their study, Improved digestibility of β-lactoglobulin by pulsed light processing, the method appeared "to facilitate digestibility" without altering the functional properties of BLG.
Improving the digestibility of BLG could in turn lower the allergenicity of milk, they speculated.
“The fact that PL treatment did not affect the functionality of the protein makes it a valuable alternative for tailoring novel food matrices with improved functional properties such as decreased digestibility, controlled energy intake and low allergenicity,” said the study.
Compact and complex structure
According to the University of Granada, BLG is responsible for around one in ten milk-related allergies.
The University of Granada's Julia Maldonado-Valderrama, one of the study's five authors, explained that BLG is difficult to digest because its compact and complex structure resists enzymatic processing during digestion.
Maldonado-Valderrama and her colleagues examined whether degrading this structure would facilitate digestion.
They were aware, however, that if the structure was severely degraded the protein would lose its functional properties.
By increasing the number of light pulses, however, they found they could degrade the structure of BLG without affecting the lactose protein's functional properties.
"We actually demonstrated that in some cases pulsed light even improves the emulsive properties of lactose protein," said Maldonado-Valderrama.
This pulsed light process has since been patented by Azti-Tecnalia.
Simulated digestion
Next, they simulated digestion of the modified protein using a device, designed and built at the University of Granada, called Octopus.
The method, the University of Granada said, "demonstrated" that pulsed light treatment facilitates digestion of BLG - particularly in the small intestine.
Concluding, Maldonado-Valderrama said: "Finding a way of improving the digestibility of proteins without altering their functional properties is a current challenge within food technology and, in this respect pulsed light treatment is a very promising tool when it comes to the design of low-allergy food product.”
Source: Soft Matter 10.1039/C4SM01667J
Title: Improved digestibility of β-lactoglobulin by pulsed light processing: a dilatational and shear study.
Authors: T del Castillo-Santealla, E Sanmartin, MA Cabrerizo-Vilchez, JC Arboleya, J Maldonado-Valderrama.