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2,4-Hexadienoic acid, 2-hydroxy- is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

219488-73-0

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219488-73-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 219488-73-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,1,9,4,8 and 8 respectively; the second part has 2 digits, 7 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 219488-73:
(8*2)+(7*1)+(6*9)+(5*4)+(4*8)+(3*8)+(2*7)+(1*3)=170
170 % 10 = 0
So 219488-73-0 is a valid CAS Registry Number.

219488-73-0Downstream Products

219488-73-0Relevant academic research and scientific papers

Catalytic transformation of HODAs using an efficient meta-cleavage product hydrolase-spore surface display system

Qu, Yuanyuan,Wang, Jingwei,Zhang, Zhaojing,Shi, Shengnan,Li, Duanxing,Shen, Wenli,Shen,Zhou, Jiti

, p. 204 - 210 (2014)

The accumulation of 2-hydroxy-6-oxohexa-2,4-dienoic acids (HODAs) in the process of aromatics transformation will hinder the mineralization rate. In this study, a novel type of biocatalyst, meta-cleavage product (MCP) hydrolase (MfphA and BphD) displayed on the surface of Bacillus subtilis 168 spores, was developed for the transformation of HODAs. The successful display of CotG-MfphA and CotG-BphD fusion protein on the surface of spore were confirmed by western blot analysis and activity measurement. The optimal transformation conditions by spore surface-displayed MfphA and BphD were found to be 70 C and pH 7. The thermal and pH stability analysis exhibited that spore surface-displayed MfphA and BphD were stable and retained more than 80% of relative activities even at 80 C and pH 10. Meanwhile, recycling experiments showed that the conversion percentage of HODA by surface-displayed MfphA and BphD were not significantly decreased throughout the reutilization process, which still retained 45% and 70% at the tenth cycle, respectively. To the best of our knowledge, this is the first report concerning the B. subtilis 168 spore surface-displayed MCP hydrolases. The high activities and good recycle performance suggested that this novel biocatalyst system could serve as a suitable alternative for HODAs transformation.

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