Data/hora: 14/06/2024 03:37:14

Biblioteca(s): 	Embrapa Agroindústria de Alimentos.	
Data corrente: 	20/09/2017	
Data da última atualização: 	08/03/2024	
Autoria: 	SANTOS, M. B.; CARVALHO, C. W. P. de; GARCIA-ROJAS, E. E.	
Afiliação: 	MONIQUE BARRETO SANTOS, UNIVERSIDADE FEDERAL RURAL DO RIO DE JANEIRO; CARLOS WANDERLEI PILER DE CARVALHO, CTAA; EDWIN ELARD GARCIA-ROJAS, UNIVERSIDADE FEDERAL FLUMINENSE.	
Título: 	Heteroprotein complex formation of bovine serum albumin and lysozyme: Structure and thermal stability.	
Ano de publicação: 	2018	
Fonte/Imprenta: 	Food Hydrocolloids, n. 74, p. 267-274, 2018.	
Idioma: 	Inglês	
Conteúdo: 	The formation of a heteroprotein complex obtained by the interaction of bovine serum albumin (BSA) and lysozyme (Lys) was investigated by pH variation using turbidimetric analysis and zeta potential (ζ) at different protein ratios and NaCl concentrations. The complexes were formed in a pH range between 8.0 and 11.0, with the ratio r = 0.5 at pH 9.0 presenting the highest complexation. The addition of NaCl decreased the interaction at concentrations of 10 mM. The complex formation occurred between the isoelectric points (pI) of the proteins, close to a balance of charges, mainly by electrostatic interactions with some participation of hydrogen bonds. Differential scanning calorimetry suggested that the interaction gave rise to a new biopolymer due to the formation of a single denaturation point at 67 °C. The structures formed had an average size of ∼1.7 μm, well above that of the isolated proteins, and microscopic analysis revealed that the complexes had a globular structure. BSA/Lys complexes may be a potential bioactive encapsulating agent and may be used as a food ingredient.	
Palavras-Chave: 	Coacervation; Differential scanning; Electrostatic interaction; Globular proteins; Microencapsulating.	
Thesaurus Nal: 	calorimetry.	
Categoria do assunto: 	X Pesquisa, Tecnologia e Engenharia	
Registro original: 	Embrapa Agroindústria de Alimentos (CTAA)	
Exemplares: 	CTAA - (13769-1) - UPC - AP - DD -  -  -  - DIS