| Title: |
Polymerization of sorghum protein digests by transglutaminase: Changes in structure and functional properties |
| Authors: |
Mazahib Adam Mohamed; Isam A. Mohamed Ahmed; Elfadil E. Babiker; Abu Elgasim; A. Yagoub |
| Contributors: |
The Pennsylvania State University CiteSeerX Archives |
| Source: |
http://scihub.org/ABJNA/PDF/2010/1/47-55.pdf. |
| Collection: |
CiteSeerX |
| Subject Terms: |
Sorghum bicolor; protein isolate; chymotrypsin; transglutaminase; emulsifying properties |
| Description: |
Two sorghum cultivars, Tababt (low tannin) and Wad Ahmed (high tannin) were employed for this study. Difference in protein content between the cultivars was observed. Amino acid composition showed that the cultivars were rich in glutamic acid and deficient in lysine. The proteins of the two cultivars was isolated and digested by chymotrypsin. Then, the native and digested proteins were polymerized by microbial transglutaminase (TGase). Structural and functional properties of the native, digested and polymerized proteins were also investigated. SDS-PAGE pattern of the polymerized proteins showed that, TGase treatment resulted in proteins of higher molecular mass above the stacking gel, indicating that the enzyme catalyses the cross link of the protein units even after digestion. Moreover, the free amino groups of the polymerized proteins were greatly reduced. The native and chymotrypsin digested protein were found to be soluble at acid and alkaline pH, with the lowest solubility observed at pH 4. The solubility of the protein digest polymer improved significantly at all pH levels, with the shift of the lowest solubility to pH 6. The protein polymer started to coagulate when the heating temperature exceeded 50oC. The digest polymer, on the other hand, resisted heat-induced aggregation up to 60oC; thereafter, its solubility |
| Document Type: |
text |
| File Description: |
application/pdf |
| Language: |
English |
| Relation: |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.466.1979 |
| Availability: |
http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.466.1979; http://scihub.org/ABJNA/PDF/2010/1/47-55.pdf |
| Rights: |
Metadata may be used without restrictions as long as the oai identifier remains attached to it. |
| Accession Number: |
edsbas.1F7742B2 |
| Database: |
BASE |