Characterization of pronase digestion rate and products of protein meals


Citation

Karossi T.A., . and Sutherland T.M., . Characterization of pronase digestion rate and products of protein meals. pp. 64-70. ISSN 0127-7324

Abstract

Nitrogen digestibility in vitro of common protein meals assessed with prolonged incubation with pronase was studied. Digestible available-lysine determination using 2 4 6-TNBS reagent were included in the studies. Exclusion chromatography on sephadex G-25 of the pronatic digests indicated that in no case had the pronase digestion converted the protein in quantity to the molecular weight range needed for intestinal absorption although a large part had been converted to the range below 1000 Daltons. Deproteinization with picric acid although in general tending to remove higher peptides showed no clear cut off and left in solution some oligopeptides larger than 1000 Daltons. The insoluble residues from the pronase treatment were tested separately with pronase trypsin alpha-ahymotrypsin S. griseus protease collagenase and pepsin and in general showed s0925usceptibility to further proteolysis. Kinetic studies with simultaneous hydrolysis of the test proteins and dialysis to remove the products of hydrolysis with pronase and initial reaction rate study with trypsin and their relationship with the molecular weight distribution were investig


Download File

Full text available from:

Abstract

Nitrogen digestibility in vitro of common protein meals assessed with prolonged incubation with pronase was studied. Digestible available-lysine determination using 2 4 6-TNBS reagent were included in the studies. Exclusion chromatography on sephadex G-25 of the pronatic digests indicated that in no case had the pronase digestion converted the protein in quantity to the molecular weight range needed for intestinal absorption although a large part had been converted to the range below 1000 Daltons. Deproteinization with picric acid although in general tending to remove higher peptides showed no clear cut off and left in solution some oligopeptides larger than 1000 Daltons. The insoluble residues from the pronase treatment were tested separately with pronase trypsin alpha-ahymotrypsin S. griseus protease collagenase and pepsin and in general showed s0925usceptibility to further proteolysis. Kinetic studies with simultaneous hydrolysis of the test proteins and dialysis to remove the products of hydrolysis with pronase and initial reaction rate study with trypsin and their relationship with the molecular weight distribution were investig

Additional Metadata

[error in script]
Item Type: Article
Additional Information: Ill.; 7 tables; 31 ref. Summary (En)
AGROVOC Term: edPRODUCTOS PROTEINICOS
AGROVOC Term: DIGESTIBILIDAD
AGROVOC Term: NITROGENO
AGROVOC Term: CROMATOGRAFIA/ PROTEASAS
AGROVOC Term: PREPARACION ENZIMATICA
AGROVOC Term: ACTIVIDAD ENZIMA
Depositing User: Ms. Norfaezah Khomsan
Last Modified: 24 Apr 2025 05:54
URI: http://webagris.upm.edu.my/id/eprint/19352

Actions (login required)

View Item View Item