Asian Science Citation Index is committed to provide an authoritative, trusted and significant information by the coverage of the most important and influential journals to meet the needs of the global scientific community.  
ASCI Database
308-Lasani Town,
Sargodha Road,
Faisalabad, Pakistan
Fax: +92-41-8815544
Contact Via Web
Suggest a Journal
Articles by Issoufou Amadou
Total Records ( 3 ) for Issoufou Amadou
  Mahomed Beva Kelfala Foh , Issoufou Amadou , Mohamed Tabita Kamara , Betty Mabel Foh and Wenshui Xia
  In this study, we examined the effects of enzymatic hydrolysis on the functional and nutritional properties of Nile tilapia (Oreochromis niloticus) proteins. Nile tilapia was enzymatically hydrolyzed by several commercially available proteases (Alcalase 2.4 L, Neutrase and Flavourzyme), with protein recovery of 89.86, 81.92 and 73.12%, respectively. The hydrolysates were prepared with 1% enzymes/substrate ratio (E/S). Essential amino acids were above the recommended amount by Food and Agricultural Organization/World Health Organization for humans. Lower molecular weights were more predominant in Hot Water Dip Hydrolysates (HWDH) whose peaks ranged from 328- 1876 Da. Furthermore, the Hot Water Dip Concentrates (HWDC) were mainly composed of higher molecular weight (214-19,576 Da). HWDH and HWDC have varied solubilities above 80% at pH 12.0. Hydrophobicities of 168.01 and 200.28, water-binding capacity was in the range of 1.77 and 2.43 mL g-1 while oil absorption capacity ranged between 2.23 and 3.36 g mL-1, bulk density of 0.53 and 0.36 mL g-1 and emulsifying capacity of 21.40 and 20.40 mL 0.5 g-1 for both HWDH and HWDC, respectively. Foam capacity and foam stability ranged from 124.53 to 37.25 mL g-1 for HWDH and from 80.3 to 45.57 mL g-1 for HWDC. The hydrolysate was more easily digestible than the concentrate with a significant difference (p<0.05). All the estimated nutritional parameters based on amino acids composition suggested that Nile tilapia protein hydrolysates and concentrates have good nutritional quality and could be used as protein ingredient in food industries.
  Abdoulaye Sankhon , Wei-Rong Yao , Issoufou Amadou , Heya Wang , He Qian and Moustapha Sangare
  This study describes the isolation, digestibility and effect of process conditions on the Parkia biglobosa (African locust bean) starch digestibility. Parkia starch fractions are: Total Starch (TS), Rapidly Digestible Starch (RDS), Slowly Digestible Starch (SDS) and Resistant Starch (RS). The results indicate that processing conditions can be changed to effectively control the relative content of SDS and RS in Parkia starch products. Amylose is the molecular basis of RS while amylopectin is the main constituent of SDS and plays a key role in the structure and digestibility of SDS. This methodology may enable process modifications to influence the functional digestibility properties of prepared Parkia starch products.
  Issoufou Amadou , Olasunkanmi S. Gbadamosi , Yong- Hui Shi , Mohamed T. Kamara , Sun Jin and Guo-Wei Le
  In this study, we previously reported that peptides fractions obtained by gel filtration chromatography from Fermented Soybean Protein Meal Hydrolysate (FSPMH) showed strong antioxidative activity. In this study we particularly focused on the fraction F2 which showed the highest antioxidant properties. The fraction F2 was subjected to reverse phase high performance liquid chromatography (RP-HPLC) for purification. The resultant peaks were collected separately as fractions and subsequently subjected to DPPH radical scavenging and Cu2+ chelating tests. The amino acid sequences of isolated peptides were then determined by liquid chromatography/tandem mass spectrometry (LC-MS/MS). The RP-HPLC fraction P1 showed stronger 1, 1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging ability and possessed relatively strong Cu2+ chelation ability compared to 5 other RP-HPLC fractions. The amino acid sequences indicated that the isolated peptides contained Histidine.
Copyright   |   Desclaimer   |    Privacy Policy   |   Browsers   |   Accessibility