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<article article-type="research-article" dtd-version="1.3" xmlns:xlink="http://www.w3.org/1999/xlink">
	<front>
		<journal-meta>
			<journal-title-group>
				<journal-title>Tạp chí Khoa học và Công nghệ</journal-title>
				<abbrev-journal-title>Khoa học &amp; Công nghệ</abbrev-journal-title>
			</journal-title-group>
			<issn pub-type="ppub">2615-9015</issn>
			<issn pub-type="epub">2615-9015</issn>
			<publisher><publisher-name>Trường Đại học Nguyễn Tất Thành</publisher-name></publisher>
		</journal-meta>
		<article-meta>
			<article-id pub-id-type="publisher-id">04b679f6-fb59-83ad-9742-01a0fbabc91a</article-id>
			<article-id pub-id-type="doi">10.55401/thk7jy59</article-id>
			<title-group><article-title>Recombinant protein expression of Magnaporthe oryzae MGG06069 and its polysaccharide monooxygenase domain in Escherichia coli</article-title></title-group>
			<contrib-group>
				<contrib contrib-type="author"><string-name>Bui Cong Chinh</string-name></contrib><contrib contrib-type="author"><string-name>Ho Ta Giap</string-name></contrib><contrib contrib-type="author"><string-name>Vu Van Van</string-name></contrib>
			</contrib-group>
			<pub-date pub-type="epub"><day>24</day><month>1</month><year>2024</year></pub-date>
			<volume>5</volume>
			<issue>1</issue>
			<fpage>1</fpage>
			<lpage>5</lpage>
			<self-uri content-type="html" xlink:href="https://jst.ntt.edu.vn/articles/04b679f6-fb59-83ad-9742-01a0fbabc91a" />
			<self-uri content-type="pdf" xlink:href="https://uploadservice.ntt.edu.vn/dbOBrwZN1R_1/file/1_recombinant_protein_expression_of_magnaporthe_261002-Br1xT6ZmxtCg.pdf" />
			<abstract><p>MGG06069 is a polysaccharide monooxygenase protein that originated from the fungusthat causes rice blast, Magnaporthe oryzae. It has the potential to speed up thecellulolysis process, which can be beneficial for industry. In this study, the full-lengthMGG06069 protein and its polysaccharide monooxygenase domain were expressed inEscherichia coli in order to produce recombinant proteins on a large scale for furtherenzymatic experiment. It was shown that the amount of the recombinant polysaccharidemonooxygenase domain protein was much higher compared to that of the full-lengthprotein. In addition, only one band of expected size was obtained for the recombinantPMO domain protein. These results suggest the purified polysaccharidemonooxygenase domain of MGG06069 that can be used for enzymatic assaysin the future.</p></abstract>
			<kwd-group><kwd>AA9</kwd><kwd>MGG06069</kwd><kwd>Escherichia coli</kwd><kwd>Polysaccharide Monooxygenase</kwd><kwd>PMOs</kwd></kwd-group>
		</article-meta>
	</front>
</article>