Proteins are the main constituent materials of organisms, and the three-dimensional structure of proteins is the key to the function of proteins. However, the three-dimensional structure of proteins can be damaged by sensitive reactions due to slight environmental changes such as temperature and acidity. However, proteins produced by microorganisms living in an environment near the boiling temperature of hot springs have a high degree of thermal stability.
Ningxia
Kofolon International Co.,Ltd make and export Frozen Horseradish roots.We have our horseradish planting base with
5000 acres.Our frozen horseradish roots is used for Japanese
food,sea food and fashion food. Our frozen horseradish roots is healthy,natural,spicy and
delicious, and very popular in Japan,Korea,America,Europe,Brazil,Taiwan,South-East
Asia,etc.
We
can make frozen horseradish roots as your
request,such as quality,price,packing,color,etc.
More
details is following.
Packing:15kgs/CTN 25tons/40`RH
Ingredients:horseradish
Delivery:20
days
MOQ:25TONS
Payment:T/T
Frozen Horseradish Frozen Horseradish,Frozen Diced Horseradish,Dried Frozen Horseradish,Raw Material Horseradish NINGXIA KOFOLON INTERNATIONAL CO.,LTD. , http://www.kofolon.com
A research team headed by Mr. Yoshiko K. Yoshiaki of the Institute of Radiological Science at the Haruo Research Institute of the Japan Institute of Physical and Chemical Research conducted a study on a protein called “Cué„„tA1â€, a thermophilic protein, and found that the protein was exposed to 148.5 degrees Celsius. To destroy. This discovery is 30 degrees Celsius higher than the highest heat-resistant temperature of the currently known heat-resistant proteins and is the most heat-resistant protein found so far.
The "CutA1" protein is widely found in microorganisms, plants and animals. Human brain cells also contain this protein. Through the analysis of the three-dimensional structure of this protein, the team also found that the ionic bond on the surface of the protein molecule is the key to maintaining thermal stability. The ionic bonds that cover the surface of protein molecules form a network that functions as an insulating material. The research team observed the thermal decomposition process under various conditions and found that the three-dimensional structure of the protein can inhibit the thermal decomposition of amino acid residues and maintain the shape of the protein at a high temperature of approximately 150 degrees Celsius.
This discovery has an important role in the design of high-heat-resistant proteins and the analysis of the function of abnormal Prio proteins in vivo. The results of this study will be published on the European Biochemistry Bulletin on July 24.