Evaluation of tinospora cordifolia amylase as a commercial digestive enzyme of plant origin

Abstract

Tinospora cordifolia stem contained 470 + 50, 3.0 + 1.5, and 1.5 + 0.5 units of amylase, maltase, and isomaltase, respectively, per gram of fresh tissue. Amylase was more thermo- and acid-stable than fungal, porcine pancreatic and human salivary amylases and liberated much more reducing sugar and glucose from cerea starches, amylopectin and glycogen than fungal enzyme. Crude enzyme hydrolyzed maltose, isomaltose, raffinose, melezitose and raw starch and therefore does not require the participation of intestinal disaccharidases for complete digestion of dietary starch into glucose. The enzyme protein was nontoxic at an oral dose of 1.5 g.Kg-1 body weight.