Background: Pharmaceutical excipients are traditionally inert carriers, but the concept of "functional excipients" - inactive ingredients that provide additional therapeutic or stability benefits - is gaining traction. Digestive enzymes from insect sources represent an underexplored category of such excipients.

Objective: This study aimed to extract, partially purify, and characterize trypsin and α-amylase from the common field cricket Gryllus campestris, and evaluate their potential as pharmaceutical excipients.

Methods: Crickets were homogenized, and enzymes were extracted using cold phosphate-buffered saline. Ammonium sulphate fractionation (30-70% saturation) and dialysis were employed for partial purification. Trypsin activity was assayed using BAPNA substrate, and amylase using the DNS method. Biochemical characterization included pH and temperature optima, stability profiles, and kinetic parameters (Km, Vmax). SDS-PAGE and zymography confirmed molecular weights and activity. Lyophilization with maltodextrin and compatibility with common tablet excipients (lactose, microcrystalline cellulose, magnesium stearate) were assessed.

Results: Partial purification achieved 3.7-fold purification for both enzymes with ~70% activity recovery. Trypsin showed optimal activity at pH 8.0 and 45°C, while amylase was optimal at pH 6.8 and 40°C. Both enzymes retained >80% activity at 37°C for 2 hours. Km values were 0.42 mM (trypsin with BAPNA) and 1.8 mg/mL (amylase with starch). Molecular weights were approximately 24 kDa (trypsin) and 55 kDa (amylase). Lyophilization with maltodextrin (1:2 w/w) preserved >85% activity. Both enzymes showed excellent compatibility with lactose and MCC (>94% residual activity), and acceptable compatibility with magnesium stearate (>85%).