Abstract
Milk is a nutritious perishable product having a short shelf-life owing to the occurrence of spoilage bacteria in it. This has led to an increasing demand for ensuring safety through milk processing. Conventional techniques (such as heat treatment) increase shelf-life but damage the nutritional and sensory qualities of milk. Hence, there is a need to develop innovative, nonthermal processing techniques that increase the shelf-life while preserving its nutritional quality. This review focuses on the recent advances in assuring microbial safety of milk by using nonthermal techniques such as high-pressure processing, pulsed electric fields, ultrasound, ultraviolet irradiation and membrane microfiltration.
Highlights
Milk is a perishable food having high moisture contents and all nutrients that helps microorganisms to proliferate
When skim milk is subjected to High-Pressure Processing (HPP) treatment (300 MPa), it was found that the particles size substantially decreases, with the decrease of average size from about 200 to 100 nm regardless of temperature during pressurization
After HPP treatment, there is no increase in lipolysis, but some whey proteins were absorbed into the milk fat globule membrane (MFGM) and the membrane remains undamaged (Naik et al, 2013)
Summary
Milk is a perishable food having high moisture contents and all nutrients that helps microorganisms to proliferate. Thermal treatment of milk can destroy the amount of some nutritional components along with some undesirable flavour changes Considering these nutritional and organoleptic changes, novel nonthermal technologies (including high-pressure processing (HPP), pulsed electric field (PEF), ultrasound, ultraviolet irradiations, nonthermal plasma (cold plasma) and membrane microfiltration) have been developed with ability to inactivate both the pathogenic and spoilage microorganisms (Claeys et al, 2013; Amaral et al, 2018; Guimarães et al, 2018, 2019; Coutinho et al, 2019a, b; Zia et al, 2019; Aadil et al, 2018, 2020). It causes irreversible changes in secondary, tertiary and quaternary structures of protein by affecting mostly the covalent bonds (Dhakal et al, 2014)
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