F
Francisco Millán
Researcher at Spanish National Research Council
Publications - 127
Citations - 5220
Francisco Millán is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Hydrolysate & Plant protein. The author has an hindex of 38, co-authored 119 publications receiving 4471 citations.
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Protein isolates from chickpea (Cicer arietinum L.): chemical composition, functional properties and protein characterization
TL;DR: Isolate-A showed a partial dissociation of the 11S protein because of the high pH used for the protein extraction, and this probably explains the differences observed in the functional characteristics of both isolates.
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Production of ace inhibitory peptides by digestion of chickpea legumin with alcalase
María del Mar Yust,Justo Pedroche,Julio Girón-Calle,Manuel Alaiz,Francisco Millán,Javier Vioque +5 more
TL;DR: In this article, the authors showed that legumin with alcalase yielded a hydrolysate that inhibited the angiotensin I-converting enzyme with an IC 50 of 0.18 mg/ml.
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Purification of an ACE inhibitory peptide after hydrolysis of sunflower (Helianthus annuus L.) protein isolates.
Cristina Megías,María del Mar Yust,Justo Pedroche,Hassan Lquari,Julio Girón-Calle,Manuel Alaiz,Francisco Millán,Javier Vioque +7 more
TL;DR: Results show that sunflower seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with pepsin and pancreatin.
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Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: Correlation between enzyme–support linkages and thermal stability
Justo Pedroche,María del Mar Yust,Cesar Mateo,Roberto Fernandez-Lafuente,Julio Girón-Calle,Manuel Alaiz,Javier Vioque,Jose M. Guisan,Francisco Millán +8 more
TL;DR: It was observed that the number of lysine residues that took part in the immobilization process was a consequence of the type of support and reaction time of the experimental conditions, and that the increasing of the thermal stability of the derivatives was correlated with a increasing number ofLysines residues involved in a multipoint covalent attachment.
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Partially hydrolyzed rapeseed protein isolates with improved functional properties
TL;DR: In this paper, limited rapeseed protein hydrolysates ranging from 3.1 to 7.7% hydrolysis were produced from isoelectric-pre-cipitated protein isolate.