Exploring protein-mediated quality control mechanisms in Rice cooking behavior: from static protein content to dynamic architecture.

Abstract

Rice proteins significantly influence cooking properties and eating quality, yet their dynamic roles during thermal processing remain unclear. This study systematically investigated protein-mediated mechanisms in rice cooking through in-situ structural analysis (SEM, CLSM) and enzymatic hydrolysis. Three rice cultivars with a common genetic background but differing in protein content were used (NJ > LSS-1 > LSS-2: 6.12 %, 7.20 %, and 8.15 %), and the results demonstrated that higher protein content correlated with denser protein networks, restricted starch gelatinization evidenced by retained 1047/1022 cm-1 ratios. Protein aggregation inhibited water absorption during soaking, hydration at early steaming, and high-temperature gelatinization. The adhered layer mass significantly increased under protease treatment (0 %-5.0 %), rising from 0.35 to 0.91 g/25 g. A negative correlation (r = -0.30*, p < 0.05) between adhesion layer mass of protein and hardness highlighted protein-dependent texture regulation. These findings elucidate a three-stage protein regulation mechanism in rice cooking and propose protein modification as a strategy to tailor texture for consumer preferences.