Konjac glucomannan (KGM) is a naturally occurring macromolecular polysaccharide that exhibits remarkable film–forming and gel–forming properties, and a high degree of biocompatibility and biodegradability. The helical structure of KGM is maintained by the acetyl group, which plays a crucial role in preserving its structural integrity. Various degradation methods, including the topological structure, can enhance the stability of KGM and improve its biological activity. Recent research has focused on modifying KGM to enhance its properties, utilizing multi–scale simulation, mechanical experiments, and biosensor research. This review presents a comprehensive overview of the structure and properties of KGM, recent advancements in non–alkali thermally irreversible gel research, and its applications in biomedical materials and related areas of research. Additionally, this review outlines prospects for future KGM research, providing valuable research ideas for follow–up experiments.

Konjac glucomannan (KGM) is a natural polysaccharide extracted from konjac tubers that has a topological structure composed of glucose and mannose. KGM can be used as a gel carrier to load active molecules in food preservation. The three-dimensional gel network structure based on KGM provides good protection for the loaded active molecules and allows for sustained release, thus enhancing the antioxidant and antimicrobial activities of these molecules. KGM loaded with various active molecules has been used in aquatic foods preservation, with great potential for different food preservation applications. This review summarizes recent advances in KGM, including: (i) structural characterization, (ii) the formation mechanism, (iii) preparation methods, (iv) functional properties and (v) the preservation of aquatic food.

L. vannamei has become one of the most productive species. However, it is susceptible to microbial contamination during fishing, transportation, and storage, which can lead to spoilage and quality deterioration. This study investigates the relationship between changes in the proteome of Litopenaeus vannamei (L. vannamei) muscle and quality characteristics during low-temperature storage using the tandem mass spectrometry technology of quantitative proteomics strategy. The differential expression of proteins under cold storage (4 °C, CS), partial slight freezing (−3 °C, PFS), and frozen storage (−18 °C, FS) conditions was compared with the fresh group (CK), resulting in 1572 proteins identified as differentially expressed. The purpose of this research is to identify potential biochemical markers by analyzing quality changes and relative differential proteins through searches in the UniProt database, Gene Ontology database, and Genome Encyclopedia. Correlation analysis revealed that seven DEPs were significantly related to physical and chemical indicators. Bioinformatics analysis demonstrated that most DEPs are involved in binding proteins, metabolic enzymes, and protein turnover. Additionally, some DEPs were identified as potential biomarkers for muscle decline. These findings contribute to understanding the mechanism of freshness decline in L. vannamei under low-temperature storage and the changes in muscle proteome.