- “A genomic library was constructed to clone a xylanase gene (Mxyn10) from Demequina sp. JK4 isolated from a deep sea.”1
Researchers from State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, in Wuhan, Hubei, China; College of Plant Science and Technology, Huazhong Agricultural University, in Wuhan, Hubei, China; and Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State of Oceanic Administration, Xiamen (Amoy), Fujian, China; have presented an article titled: “A Novel pH-Stable, Bifunctional Xylanase Isolated from a Deep-Sea Microorganism, Demequina sp. JK4.”
The researchers from Wuhan, Hubei, and from Xiamen, Fujian, have also noted:
- “Mxyn10 encoded a 471 residue protein with a calculated molecular mass of 49 kDa.”
- “This protein showed the highest sequence identity (70%) with the xylanase from Streptomyces lividans.”
- “Mxyn10 contains a catalytic domain that belongs to the glycoside hydrolase family 10 (GH10) and a carbohydrate-binding module (CBM) belonging to family 2.”
- “The optimum pH and temperature for enzymatic activity were pH 5.5 and 55 degrees , respectively.”
- “Mxyn10 exhibited good pH stability, remaining stable after treatment with buffers ranging from pH 3.5 to 10.0.”
- “The protein was not significantly affected by a variety of chemical reagents, including some compounds that usually inhibit the activity of other related enzymes.”
- “In addition, Mxyn10 showed activity on cellulose.”
- “These properties mark Mxyn10 as a potential enzyme for industrial application and saccharification processes essential for bioethanol production.”
