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Its genome contains several putative carbohydrate\u2010active enzymes such as glycoside hydrolases and lytic polysaccharide monooxygenases (PMOs). In this study, we have heterologously produced in <jats:italic>Escherichia coli<\/jats:italic> and characterized a new enzyme belonging to the AA10 family, named <jats:italic>Pp<\/jats:italic>AA10 (Uniprot: B1J2U9), which contains a chitin\u2010binding type\u20104 module and showed activity toward \u03b2\u2010chitin. The active form of the enzyme was produced in <jats:italic>E. coli<\/jats:italic> exploiting the addition of a cleavable N\u2010terminal His tag which ensured the presence of the copper\u2010coordinating His as the first residue. Electron paramagnetic resonance spectroscopy showed signal signatures similar to those observed for the copper\u2010binding site of chitin\u2010cleaving PMOs. The protein was used to develop a versatile, highly sensitive, cost\u2010effective and easy\u2010to\u2010apply method to detect PMO's activity exploiting attenuated total reflection\u2010Fourier transform infrared spectroscopy and able to easily discriminate between different substrates.<\/jats:p>","DOI":"10.1002\/pro.4255","type":"journal-article","created":{"date-parts":[[2021,12,12]],"date-time":"2021-12-12T06:34:50Z","timestamp":1639290890000},"page":"591-601","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Activity and substrate specificity of lytic polysaccharide monooxygenases: An <scp>ATR FTIR<\/scp>\u2010based sensitive assay tested on a novel species from <i>Pseudomonas putida<\/i>"],"prefix":"10.1002","volume":"31","author":[{"given":"Ilenia","family":"Serra","sequence":"first","affiliation":[{"name":"Department of Life Sciences University of Modena and Reggio Emilia  Modena 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