@article{oai:oacis.repo.nii.ac.jp:00001787,
 author = {Wang, Shaohua and Yang, Ying and Zhang, Jian and Sun, Jiaqi and Matsukawa, Shingo and Xie, Jingli and Wei, Dongzhi},
 issue = {14},
 journal = {Bioresources and Bioprocessing},
 month = {Sep},
 note = {Background: Protopectinases which were consisted of various different enzymes can promote the solubilization of protopectin from the plant cell and can be applied in the protein industry extraction. The genome sequence of Paenibacillus polymyxa Z6 that produces a protopectinases complex was partially determined. Two new genes, yxiA1 and yxiA3, were identified as uncharacterized protein in the P. polymyxa genome. And, they were classified as the member of the glycoside hydrolase family 43 (GH43) according to the primary protein sequence., Results: The two genes were cloned and expressed in Escherichia coli BL21 (DE3). And, the results indicated that the product of yxiA1 and yxiA3 were two endo-α-1,5-l-arabinanases. Thus, the two genes were renamed as abnZ2 (yxiA1) and abnZ3 (yxiA3). Recombinant AbnZ2 had optimal activity at pH 6.0 and 35°C. And, AbnZ3 had optimal activity at pH 6.0 and 30°C. However, unlike most reported endo-arabinanases, the specific activity of AbnZ3 remained 48.7% of maximum at 5°C, which meant AbnZ3 was an excellent cold-adapted enzyme., Conclusions: This paper demonstrated that the gene yxiA1 and yxiA3 were two new endo-arabinanases, and renamed as abnZ2 and abnZ3. Moreover AbnZ3 was an excellent cold-adapted enzyme which could be attractive in fruit juice processing., 26282017},
 title = {Characterization of abnZ2 (yxiA1) and abnZ3 (yxiA3) in Paenibacillus polymyxa, encoding two novel endo-1,5-α-l-arabinanases},
 volume = {1},
 year = {2014}
}