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Preparation and function of oligopeptide-enriched hydrolysate from globin by pepsin

Paper ID Volume ID Publish Year Pages File Format Full-Text
36420 45132 2006 5 PDF Available
Title
Preparation and function of oligopeptide-enriched hydrolysate from globin by pepsin
Abstract

Animal blood is potentially an untapped source of drugs and value-added food production. More than 400 million pigs are slaughtered each year but porcine blood is usually discarded in China. In this paper, globin derived from porcine hemoglobin was digested by pepsin, then the hydrolysate was separated on Sephadex LH-20 gel filtration column and five major fractions (I, II, III, IV and V) were obtained. Biological functions of the hydrolysate and five fractions were assayed. The hydrolysate and fractions IV and V had good angiotensin-I-converting enzyme inhibitory activity, with IC50 values of 1.19, 0.67, 0.10 mg/ml, respectively. Fractions I, II, III, IV showed no significant α-glucosidase inhibitory activity, but fraction V showed appreciably stronger activity than acarbose at the same concentration. Thus, the study has shown that porcine blood can be utilized to generate high value-added products, ACE inhibitory peptides and α-glucosidase inhibitory peptides.

Keywords
Globin; Angiotensin-I-converting enzyme; α-Glucosidase; Inhibitory activity
First Page Preview
Preparation and function of oligopeptide-enriched hydrolysate from globin by pepsin
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 41, Issue 7, July 2006, Pages 1589–1593
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering