Abstract
Abstract A psychrophilic and halophilic bacterial isolate, Shewanella sp. ISTPL2, procured from the pristine Pangong Lake, Ladakh, Jammu and Kashmir, India, was used for the production and characterization of the psychrophilic and alkalophilic α-amylase enzyme. The α-amylase is a critical enzyme that catalyses the hydrolysis of α-1,4-glycosidic bonds of starch molecules and is predominately utilized in biotechnological applications. The highest enzyme activity of partially purified extracellular α-amylase was 10,064.20 U/mL after 12 h of incubation in a shake flask at pH 6.9 and 10 °C. Moreover, the maximum intracellular α-amylase enzyme activity (259.62 U/mL) was also observed at 6 h of incubation. The extracellular α-amylase was refined to the homogeneity with the specific enzyme activity of 36,690.47 U/mg protein corresponding to 6.87-fold purification. The optimized pH and temperature for the α-amylase were found to be pH 8 and 4 °C, respectively, suggesting its stability at alkaline conditions and low or higher temperatures. The amylase activity was highly activated by Cu2+, Fe2+ and Ca2+, while inhibited by Cd2+, Co2+ and Na2+. As per our knowledge, the current study reports the highest activity of a psychrophilic α-amylase enzyme providing prominent biotechnological potential.
Highlights
Enzymes are complex biocatalysts that accelerate the metabolic reactions of a biological system [1]
The current study reports the highest activity of a psychrophilic α-amylase enzyme providing prominent biotechnological potential
procured from the pristine Pangong Lake (ISTPL2) was employed for the production, optimization and characterization of the α-amylase enzyme
Summary
Enzymes are complex biocatalysts that accelerate the metabolic reactions of a biological system [1]. Amylose is a linear α-1,4-glucan, while amylopectin is a branched polymer with α-1,6-glucosidic linkages in the structure The ratio of both constituents (amylose : amylopectin) depends on the origin of starch, while the general levels are always around 1:3 [6]. Α-Amylase is, in general, an enzyme with a vast preference for substrate and product specificity. This is one of the most commonly occurring glycoside hydrolases (GHs) in the sequencebased classification system of all carbohydrate-active enzymes (CAZy) into GH families [9,10]. Microbial enzymes are preferred over other sources because they can be purified, are environment- and cost-friendly, of better quality and can be cultured in a controlled environment [14] Depending on their origin, amylases can be archaeal, bacterial and eukaryotic. The enzyme production is affected by culture pH, temperature, the concentration of metal ions and was optimized
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
