# Processing-Induced Modifications of Camel Milk Immunoglobulins and Lactoferrin: Implications for Immunocompromised Pediatric Populations and Therapeutic Applications

## TL;DR

Camel milk contains beneficial proteins that can help immunocompromised children, but processing methods can damage these proteins, affecting their health benefits.

## Contribution

The paper systematically reviews how processing affects camel milk proteins and proposes alternatives to preserve their bioactivity.

## Key findings

- Thermal treatments reduce the bioactivity of camel milk proteins.
- Non-thermal methods like HPP and pulsed electric fields may preserve protein function.
- More research is needed to optimize processing for both safety and bioactivity.

## Abstract

Immunocompromised pediatric populations (children with inborn errors of immunity, HIV infection, and cancer, as well as those undergoing hematopoietic stem-cell transplantation) have severe nutritional challenges, with malnutrition depending on the underlying condition. Camel milk (CM) represents a culturally accessible, high-quality nutritional parameter and functional food naturally enriched with particular immunological components such as heavy-chain antibodies that represent 75% of total immunoglobulins (IGs) and lactoferrin (LF) at a concentration 3–5 times higher than bovine milk (BM). However, there is a critical processing paradox: the thermal treatments required for the microbiological safety of immunosuppressed children who show a 20-fold greater susceptibility to foodborne pathogens degrade the therapeutic bioactive proteins. This comprehensive review provides a systematic evaluation of processing-induced modifications of CM IGs and LF, which involve thermal and non-thermal technologies, and their effects on the molecular structure and biological function. Emerging alternatives such as high-pressure processing (HPP), pulsed electric fields, and strategic fermentation show promising bioactivity retention without compromising safety. Critical knowledge gaps remain in the structure–function relationships of processed CM proteins, necessitating evidence-based optimization strategies to balance microbiological safety with clinically relevant immunomodulatory functions for vulnerable pediatric populations.