索引于
  • Genamics 期刊搜索
  • 学术钥匙
  • 期刊目录
  • 中国知网(CNKI)
  • 访问全球在线农业研究 (AGORA)
  • 国际农业与生物科学中心 (CABI)
  • 参考搜索
  • 研究期刊索引目录 (DRJI)
  • 哈姆达大学
  • 亚利桑那州EBSCO
  • OCLC-WorldCat
  • 学者指导
  • SWB 在线目录
  • 普布隆斯
  • 欧洲酒吧
  • 谷歌学术
分享此页面
期刊传单
Flyer image

抽象的

Enhancement of Non-thermal Treatment on Inactivation of Glucoamylase and Acid Protease Using CO2 Microbubbles

Pokhum C, Chawengkijwanich C and Kobayashi F

Thermal treatment is usually used for food pasteurization and enzyme inactivation. However, it has an adverse effect on the quality of thermal-sensitive food such as fruit juice, Japanese sake, milk, yogurt and jam. In this study, we presented an alternative method for a non-thermal treatment with at 45 and 50°C for glucoamylase and protease inactivation using pressurized carbon dioxide (CO2). Twelve liters of enzyme solution (0.004% glucoamylase or 0.015% protease) was fed into a low pressure (2 MPa) CO2 mixing vessel. CO2 microbubbles (MB-CO2) were generated by introducing the mixture through a swiveling microbubble generator. The mixture containing MB-CO2 was flowed to incubate in a heating coil at various conditions (temperature at 45 or 50°C and pressure 2, 4, or 6 MPa). After incubation, the mixture was sampled at 10, 20 and 30 min from the sampling valve. The relative residual activities of glucoamylase and acid protease were measured by a spectrophotometer at the absorbance of 400 nm (Abs400) and 660 nm (Abs660), respectively. Relative residual activity of glucoamylase with MB-CO2 treatment at 50°C and 4 MPa was 15.01% whereas 74.83% of glucoamylase activity was found from treatment without MB-CO2 at same temperature. For acid protease, relative residual enzyme activity with MB-CO2 treatment at 45°C and 4 MPa was 2.29% whereas that without MBCO2 treatment at 45°C was 81.25%. These results suggested that glucoamylase and acid protease could be inactivated effectively at 45 and 50°C present of MB-CO2.

免责声明: 此摘要通过人工智能工具翻译,尚未经过审核或验证