
BL Amylase
Amylase is an important hydrolase enzyme that has been widely used for many decades and represents one of the most important enzyme groups in the biotechnology field (Naidu and Saranraj, 2013). Depending upon the mechanism of reaction, catalytic activity, and structure, amylolytic enzymes are classified into three families of hydrolases: a) α-amylases (E.C. 3.2.1.2), b) β-amylases (E.C. 3.2.1.3), and glucoamylases (E.C. 3.2.1.1). Further, it can also be classified as exo- and endo-amylases (Fleuri et al., 2015). Different types of organisms, including animals, plants, and microorganisms, are the source of amylase production. Microorganisms are used for the external production of amylase. For α-amylase production, microorganisms such as Aspergillus oryzae, A. niger, Bacillus amyloliquefaciens, B. circulans, and B. licheniformis are involved. α-Amylase is used as starch saccharification in different industries and accounts for about 30% of the enzymes in the world market (Fleuri et al., 2015). In the apple juice industry, the main setbacks are turbidity, slow filtration, damage to the filtration membrane, and gelling after juice concentration due to the high starch concentration (15% of this polysaccharide). Carrin et al. (2004) used α-amylases to clarify apple juice (Granny Smith variety) at different degrees of ripeness. As amylases are calcium-containing enzymes, thus treatments with this fortify apple juices with calcium as a healthy and non-fat alternative (Dey et al., 2014). Okoth et al. (2000) used amylase before pasteurization for passion fruit juice production for increased homogeneity and decreased juice turbidity.