<p>Chronic pancreatitis is often associated with a decreased secretion of α-amylase by the pancreas. Hence, oral administration of α-amylase becomes essential; however, only a small portion of the enzyme reaches the duodenum due to inactivation of the enzyme in the gastric environment. Hence, composite gelation of pea protein and gellan [high-acyl (PP_HAG)] and [low-acyl (PP_LAG)] was studied in the presence of glucono-δ-lactone (GDL) to encapsulate and protect α-amylase from the gastric environment and facilitate a controlled in-vitro release in the intestine. The sole pea protein gel (PP) was fabricated by the pH shift and transglutaminase treatment. The pH of composite gelation was around 3.0-3.5, inducing electrostatic interactions between pea protein and gellan. Hydrogen and ionic bonds were observed in composite gels, while hydrophobic interactions were predominant in PP. A higher water holding capacity and a lower pore size, crystallinity and swelling index were observed in the composite gels. PP_HAG exhibited greater swelling in simulated gastric fluid (SGF) than in simulated intestinal fluid (SIF), while PP_LAG exhibited greater swelling in SIF. Although PP resulted in a spurt release of α-amylase, PP_LAG resulted in a sustained release in the SGF. PP_HAG on the other hand, efficiently protected α-amylase from gastric conditions and facilitated a controlled release in SIF.</p>