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Mar. Drugs 2015, 13(3), 1481-1496; doi:10.3390/md13031481

Mechanistic Insight into the Elastin Degradation Process by the Metalloprotease Myroilysin from the Deep-Sea Bacterium Myroides profundi D25

1
State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Jinan 250100, China
2
Marine Biotechnology Research Center, Shandong University, Jinan 250100, China
3
Department of Pathogenic Biology, Binzhou Medical University, Shandong Province, Yantai 264003, China
4
School of Molecular Bioscience, The University of Sydney, NSW 2006, Australia
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Takao Ojima
Received: 21 October 2014 / Accepted: 10 March 2015 / Published: 18 March 2015
(This article belongs to the Special Issue Green Chemistry Approach to Marine Products)
View Full-Text   |   Download PDF [833 KB, uploaded 18 March 2015]   |  

Abstract

Elastases have been widely studied because of their important uses as medicine and meat tenderizers. However, there are relatively few studies on marine elastases. Myroilysin, secreted by Myroides profundi D25 from deep-sea sediment, is a novel elastase. In this study, we examined the elastin degradation mechanism of myroilysin. When mixed with insoluble bovine elastin, myroilysin bound hydrophobically, suggesting that this elastase may interact with the hydrophobic domains of elastin. Consistent with this, analysis of the cleavage pattern of myroilysin on bovine elastin and recombinant tropoelastin revealed that myroilysin preferentially cleaves peptide bonds with hydrophobic residues at the P1 and/or P1′ positions. Scanning electron microscopy (SEM) of cross-linked recombinant tropoelastin degraded by myroilysin showed preferential damages of spherules over cross-links, as expected for a hydrophobic preference. The degradation process of myroilysin on bovine elastin fibres was followed by light microscopy and SEM, revealing that degradation begins with the formation of crevices and cavities at the fibre surface, with these openings increasing in number and size until the fibre breaks into small pieces, which are subsequently fragmented. Our results are helpful for developing biotechnological applications for myroilysin. View Full-Text
Keywords: deep sea; elastase; bacteria; degradation mechanism; biotechnological potential deep sea; elastase; bacteria; degradation mechanism; biotechnological potential
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Yang, J.; Zhao, H.-L.; Tang, B.-L.; Chen, X.-L.; Su, H.-N.; Zhang, X.-Y.; Song, X.-Y.; Zhou, B.-C.; Xie, B.-B.; Weiss, A.S.; Zhang, Y.-Z. Mechanistic Insight into the Elastin Degradation Process by the Metalloprotease Myroilysin from the Deep-Sea Bacterium Myroides profundi D25. Mar. Drugs 2015, 13, 1481-1496.

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