Abstract
<title>Abstract</title> <p>The transition toward sustainable food systems has accelerated the development of plant-based meat analogues (PBMAs), yet reproducing the complex texture of muscle foods remains a major challenge. Although potato protein (PPT) possesses a high-quality amino acid profile comparable to egg protein, its potential as a structuring ingredient for PBMAs remains largely underexplored. Here, we investigate whether enzymatic restructuring of PPT can provide molecular control over its gel network formation and thereby direct texture formation in plant-based meat systems. Representative enzymatic pathways, including hydrolysis, deamidation, crosslinking, and conjugation, were applied either during ingredient preparation or through in situ network curing. The extent of protein molecular modification caused by enzymatic treatment was found to govern the resulting network formation and texture quality of the PBMA prototypes. Transglutaminase-mediated modification of PPT generated high-molecular-weight aggregates, increased gel elasticity, and produced substantially harder meat analogue prototypes. Conversely, in situ protease treatment (controlled enzymatic hydrolysis) weakened protein network connectivity while reducing adhesiveness, shifting the texture profile toward that of chicken breast. Principal component analysis identified protein molecular weight and gel strength as the primary determinants of hardness and chewiness, whereas springiness and cohesiveness were associated with protein colloidal properties. Together, these results establish hierarchical structure–function relationships linking enzyme-induced molecular restructuring to macroscopic texture. This work provides a bottom-up framework for engineering plant protein networks and offers new opportunities for the rational design of next-generation meat analogues with improved sensory quality.</p>