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<p>Carbohydrates are an important energy source for two omnivorous crustacean species, marine Antarctic krill (<i>Euphausia superba</i>) and freshwater redclaw crayfish (<i>Cherax quadricarinatus</i>), and α-glucosidase is an important enzyme of the amyloid metabolism pathway in crustaceans. However, the relationship between these enzymatic characteristics and the environment of crustaceans is still unclear. In this study, two GH13 family α-glucosidases from <i>E. superba</i> (EsAG) and <i>C. quadricarinatus</i> (CqAG) were heterologously expressed and characterized. They shared 60% amino acid sequence identity and were in the same evolutionary branch as other crustaceans according to the phylogenetic tree. <i>Euphausia superba</i> lives in a lower temperature, higher pH, and higher salinity environment compared to <i>C. quadricarinatus</i>, and the differences in the enzyme characterizations of each species were related to the differences in habitat. Firstly, the optimal temperature ranges of EsAG and CqAG were 25–35&#xa0;°C and 50–55&#xa0;°C, respectively. Secondly, the optimal pH of EsAG and CqAG were 6.5 and 5.0, respectively. Thirdly, EsAG exhibited extremely high salt tolerance, while CqAG lost most of its activity in high concentrations of salt. In addition, CqAG exhibited higher substrate affinity and catalytic efficiency compared to EsAG. The two α-glucosidases could hydrolyze several natural substrates such as maltose, sucrose and starch, and displayed transglycosylation activity to maltose. These results may enhance the understanding of carbohydrate metabolism in crustaceans and provide theoretical evidence for the nutritional and environmental status of aquatic animals.</p>

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Understanding the relationship between crustacean enzymatic characteristics and habitat environment through two α-glucosidases from Antarctic krill (Euphausia superba) and redclaw crayfish (Cherax quadricarinatus)

  • 期刊论文

  • 发表日期：

    2025年11月24日

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  • Jingjing Sun,
  • Wei Wang,
  • Chengcheng Jiang,
  • Jianhua Hao

摘要

Carbohydrates are an important energy source for two omnivorous crustacean species, marine Antarctic krill (Euphausia superba) and freshwater redclaw crayfish (Cherax quadricarinatus), and α-glucosidase is an important enzyme of the amyloid metabolism pathway in crustaceans. However, the relationship between these enzymatic characteristics and the environment of crustaceans is still unclear. In this study, two GH13 family α-glucosidases from E. superba (EsAG) and C. quadricarinatus (CqAG) were heterologously expressed and characterized. They shared 60% amino acid sequence identity and were in the same evolutionary branch as other crustaceans according to the phylogenetic tree. Euphausia superba lives in a lower temperature, higher pH, and higher salinity environment compared to C. quadricarinatus, and the differences in the enzyme characterizations of each species were related to the differences in habitat. Firstly, the optimal temperature ranges of EsAG and CqAG were 25–35 °C and 50–55 °C, respectively. Secondly, the optimal pH of EsAG and CqAG were 6.5 and 5.0, respectively. Thirdly, EsAG exhibited extremely high salt tolerance, while CqAG lost most of its activity in high concentrations of salt. In addition, CqAG exhibited higher substrate affinity and catalytic efficiency compared to EsAG. The two α-glucosidases could hydrolyze several natural substrates such as maltose, sucrose and starch, and displayed transglycosylation activity to maltose. These results may enhance the understanding of carbohydrate metabolism in crustaceans and provide theoretical evidence for the nutritional and environmental status of aquatic animals.