Emulsifying properties of β-glucan-rich extracts obtained from Pleurotus ostreatus whole mushroom and stipes

In this work, aqueous fractions were extracted from the whole Pleurotus ostreatus biomass (AF) and from a waste product (RAF) generated from it in the industry (stipes) with the aim of valorizing them as emulsifying ingredients. The composition of the aqueous extracts, before and after a purificatio...

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Detalhes bibliográficos
Autores: Pérez Bassart, Zaida, Méndez, Daniel Alexander, Martínez-Abad, Antonio, López-Rubio, Amparo, Fabra, María José
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2024
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/352193
Acesso em linha:http://hdl.handle.net/10261/352193
https://api.elsevier.com/content/abstract/scopus_id/85187797140
Access Level:acceso abierto
Palavra-chave:Aqueous extractions
Creaming index
Emulsion stability
Rheology
β-glucans
Descrição
Resumo:In this work, aqueous fractions were extracted from the whole Pleurotus ostreatus biomass (AF) and from a waste product (RAF) generated from it in the industry (stipes) with the aim of valorizing them as emulsifying ingredients. The composition of the aqueous extracts, before and after a purification step (p) carried out to enrich its content in β-glucans, was correlated with the physical stability, rheological properties and microstructure of oil-in-water (O/W) emulsions. Better emulsifying properties were obtained for AFp-based emulsions (being able to incorporate greater amounts of oil phase), than for emulsions formulated with non-purified fractions. These properties can be attributed to the relatively high protein content of AFp fractions (acting at the O/W interphase) and high viscosity of the continuous phase which slowed down the oil droplet movement. The lower emulsifying properties of β-glucan extracts obtained from the stipes was ascribed to the lower content of proteins, which were less accessible to act as surface-active compounds due to the greater glucan structural complexity with which they are interacting.