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
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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
Item Type: | Article |
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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 |
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