The present work was carried out to fabricate Grass pea (Lathyrus sativus) isolated protein (GPPI) and Alyssum homolocarpum seed gum (AHSG) complex coacervate and investigate its morphological and structural properties. Formation of complex coacervates were studied by zeta potentiometry and turbidimetric analysis as function of different pHs (7.0–2.0) and GPPI to AHSG ratios (3:1 to 1:3). The critical pH values associated with the formation of soluble (pHc) and insoluble (pHϕ1) complexes, and complete dissociation (pHϕ2) at GPPI to AHSG ratio (1:1) were found to be 4.8, 4.0, and 2.5, respectively. Formation of insoluble complex coacervate was maximum at pH 3.2 and GPPI to AHSG ratio of 1:1, where the highest yield (69%) was observed. Scanning electron microscopic (SEM) demonstrated that GPPI-AHSG complex had a rough branched-like structure. Results also showed that the complexation between GPPI and AHSG were formed through the electrostatic interaction and hydrogen bonding. Circular dichroism spectroscopy (CD) indicated that the β-sheet and random coil content in GPPI increased when AHSG molecules were added to protein solution. The fading of pure peaks of GPPI and AHSG in X-Ray diffraction (XRD) patterns of GPPI-AHSG complexes confirmed the alterations in the physical state of mixture from crystalline to amorphous. GPPI-AHSG complex coacervates had lower weight loss compared to individual GPPI and AHSG.

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