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Applied and Environmental Microbiology, April 2009, p. 1838-1844, Vol. 75, No. 7
0099-2240/09/$08.00+0     doi:10.1128/AEM.02285-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Ecological Function of Myroilysin, a Novel Bacterial M12 Metalloprotease with Elastinolytic Activity and a Synergistic Role in Collagen Hydrolysis, in Biodegradation of Deep-Sea High-Molecular-Weight Organic Nitrogen{triangledown} ,{dagger}

Xiu-Lan Chen, Bin-Bin Xie, Fei Bian, Guo-Yan Zhao, Hui-Lin Zhao, Hai-Lun He, Bai-Cheng Zhou, and Yu-Zhong Zhang*

State Key Lab of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Jinan 250100, People's Republic of China

Received 6 October 2008/ Accepted 19 January 2009

Nearly all high-molecular-weight (HMW) dissolved organic nitrogen and part of the particulate organic nitrogen in the deep sea are present in hydrolysis-resistant amides, and so far the mechanisms of biodegradation of these types of nitrogen have not been resolved. The M12 family is the second largest family in subclan MA(M) of Zn-containing metalloproteases and includes most enzymes from animals and only one enzyme (flavastacin) from a human-pathogenic bacterium (Flavobacterium meningosepticum). Here, we characterized the novel M12 protease myroilysin with elastinolytic activity and collagen-swelling ability from the newly described deep-sea bacterium Myroides profundi D25. Myroilysin is a monomer enzyme with 205 amino acid residues and a molecular mass of 22,936 Da. It has the same conserved residues at the four zinc ligands as astacin and very low levels of identity (≤40%) to other metalloproteases, indicating that it is a novel metalloprotease belonging to subfamily M12A. Myroilysin had broad specificity and much higher elastinolytic activity than the bacterial elastinase pseudolysin. To our knowledge, it is the first reported elastase in the M12 family. Although it displayed very low activity with collagen, myroilysin had strong collagen-swelling ability and played a synergistic role with collagenase in collagen hydrolysis. It can be speculated that myroilysin synergistically interacts with other enzymes in its in situ biotic assemblage and that it may play an important role in the degradation of deep-sea HMW organic nitrogen.

* Corresponding author. Mailing address: State Key Lab of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Jinan 250100, People's Republic of China. Phone: 86-531-88364326. Fax: 86-531-88564326. E-mail: zhangyz{at}sdu.edu.cn

{triangledown} Published ahead of print on 5 February 2009.

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.

Applied and Environmental Microbiology, April 2009, p. 1838-1844, Vol. 75, No. 7
0099-2240/09/$08.00+0     doi:10.1128/AEM.02285-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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