Andmebaasi logo
 

Biosynthesis of glycosidase inhibitors on wheat bread wastes hydrolysate medium by Streptomyces sp. 170

Laen...
Pisipilt

Kuupäev

2019

Kättesaadavus

Ajakirja pealkiri

Ajakirja ISSN

Köite pealkiri

Kirjastaja

Abstrakt

The aim of the present study is to investigate the potential effect of bread hydrolysate as a novel nutrient medium for cultivating Streptomyces sp. 170 (S.170). Moreover, it evaluates the productivity and inhibitory activity of pancreatic α-amylase inhibitors (PAAI). Bread hydrolysate medium (BHM) and corn starch hydrolysate medium (CHM) prepared with αamylase enzyme concentrations (1.5 and 2.5 units g -1 bread) and (1.5 units g -1 corn starch), respectively were utilized in the study. The Seherde-Blair and modified Akulova methods were applied to evaluate the carbohydrates concentration and the inhibitory activity of the media respectively. Results of bread and corn media were compared to each other. Furthermore, the activity of PAAI synthesized by S.170 was compared to other Streptomyces species. The results showed a significant difference (P < 0.05) between the total simple sugars (glucose + maltose) concentration produced in CHM (27.5%) and BHM prepared with α-amylase 1.5 units (45.1%). Besides, BHM produced by α-amylase 2.5 units demonstrated the maximum total concentration of simple sugars (49.9%). In addition, 48 h of S.170 incubation were quite enough to exhibit the highest inhibitory activity (2,632 IU mL-1 ) in BHM prepared with α-amylase 2.5 units. The analysis demonstrated a non-significant difference in the inhibitory activity of PAAI in CMH (1,300 IU mL-1 ) and BMH with α-amylase 1.5 units (1,111 IU mL-1 ). Also, compared to other Streptomyces species, S.170 conferred highly active PAAI. In conclusion, BHM showed its efficiency to a great extent in the cultivation of S.170 and production of PAAI with a notable high activity.

Kirjeldus

Article

Märksõnad

bread hydrolysate medium, corn starch medium, Streptomyces sp. 170, inhibitory activity, pancreatic α-amylase inhibitors, articles

Viide