It is important to note that 2-Amino-3-methylimidazole[4,5-f]quinoline (IQ) is one of the most common heterocyclic amines (HCAs), which is a class of mutagenic/carcinogenic harmful compounds mainly found in high-protein thermal processed foods and contaminated environments. However, the pre-carcinogenic toxicity of IQ to the liver and its mechanism are poorly understood, further research is needed. In light of this, we exposed zebrafish to IQ (0, 8, 80, and 800 ng/mL) for 35 days, followed by comprehensive experimental studies. Histopathological and ultrastructural analysis showed that hepatocytes were damaged. TUNEL results showed that IQ induced apoptosis of liver cells, the expression of apoptosis factor gene was significantly increased, and the expression of Bcl-2 protein was significantly decreased. In addition, upregulated expression of the 78-kDa glucose-regulated protein (GRP78) and C/EBP homologous protein (CHOP) and endoplasmic reticulum stress (ERS)-related factors transcription levels were elevated obviously, suggesting that IQ induced ERS. Decreased protein expression of autophagy-related 5 (Atg5)-Atg12, Beclin1, and LC3-II, increased protein expression of p62, and autophagy-related factors transcription levels were significantly decreased, suggesting that IQ inhibited autophagy. Overall, our research showed that the potential harm of IQ to the liver before the occurrence of liver cancer was related to ERS and its mediated autophagy and apoptosis pathways.

Reheating alters residual molecular order and matrix architecture in retrograded starch, but these changes do not necessarily produce parallel changes in enzymic digestion. Gels of normal maize starch (NM), high-amylose maize starch (HM), and a 50/50 (w/w) NM/HM blend were stored at 4 °C for 7 d and steam-reheated to core temperatures of 50 or 80 °C. HM was less hydrolysed than NM at either temperature. At 300 min, hydrolysis reached 51.3% and 61.4% for HM at 50 and 80 °C, respectively, versus approximately 81% for NM. DSC and XRD showed that HM-containing gels retained more thermally stable ordered structures. The 50/50 blend responded differently: reheating to 80 °C lowered hydrolysis from 72.6% to 65.6% despite no corresponding increase in residual order. This inverse response coincided with lower pore area (12.8 to 4.6 m²/g), larger 4 V/A pore diameter (966 to 2623 nm), and a more continuous freeze-dried morphology, consistent with fewer fine mercury-accessible pores and internal interfaces. Overall, starch structural composition established the broad ranking of hydrolysis after reheating, whereas matrix reorganisation modified the relationship between residual order and enzymic susceptibility in the 50/50 blend. Residual molecular order alone was therefore insufficient to predict the digestion response after reheating.