Amylases are a class of enzymes that hydrolyze starch to yield low molecular weight dextrins and sugars and they play important role in the digestion of carbohydrates. Inhibition of α‐amylase along with α‐glucosidase can significantly reduce the post‐prandial increase of blood glucose and can be an important strategy in the control of blood glucose level in the type‐2 diabetic patients. Hence, pancreatic α‐amylase and gastric glucoamylases are the major therapeutic targets for the type‐2 diabetes mellitus. Amylase inhibitors are already in the market for the treatment of diabetes. Amylase inhibitors can also be used for controlling obesity. In addition to medical applications, amylase inhibitors help in the control of pests. Therefore, amylase inhibitors play an important role in the pest management. Hence, this review is focused on the biomedical applications of amylase inhibitors. In addition, sources, different types, inhibition mechanisms, and molecular aspects of amylase inhibitors are discussed.

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Bilirubin oxidase has applications in the health and environmental sectors. Hence, several attempts have been made to increase enzyme yields. However, improvements were not very high. We report here the development of a mutant strain of Myrothecium verrucaria by using UV-rays, which produced 28.8 times more enzyme compared with the parent and was higher than the yields reported in earlier submerged cultures. The mutant strain produced 35.6 times more enzyme than the parent in solid-state fermentation, which is better than that previously reported for a solid-state fermentation process. The specific activity of the enzyme produced by the mutant was higher than that of the parental enzyme. Bilirubin oxidase from both strains showed an optimum activity at pH 7 and 40°C. However, the time required to inactivate half of the initial enzyme activity at 60°C was much higher in the case of the enzyme obtained from the mutant compared with the parental enzyme. The improved thermostability of the enzyme from the mutant strain could be due to the point mutations induced during the UV irradiation, since there was no change in the mass of the enzyme compared with the parental enzyme. The bilirubin oxidase of the mutant strain degraded the bilirubin faster than the enzyme obtained from the parent under similar conditions. Faster activity of the enzyme obtained from the mutant strain could be due to its lower K (79.4 μM) compared with that of the parental enzyme (184 μM). Hence, the mutant enzyme showed a better functionality and thermostability, which will be beneficial for industrial applications.

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