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Characterization of a major xylanase purified from Lentinula edodes cultures grown on a commercial solid lignocellulosic substrate
The white-rot basidiomycete Lentinula (syn. Lentinus) edodes (Berk.) Pegler is the dominant edible mushroom cultivated on wood. The major xylanase detected in cultures grown on a commercial oak wood medium was extracted, purified, and characterized. The enzyme was a non-debranching endo- beta -D-xyl...
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Published in: | Applied microbiology and biotechnology 1990-05, Vol.33 (2), p.226-232 |
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container_title | Applied microbiology and biotechnology |
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creator | MISHRA, C FORRESTER, I. T KELLEY, B. D BURGESS, R. R LEATHAM, G. F |
description | The white-rot basidiomycete Lentinula (syn. Lentinus) edodes (Berk.) Pegler is the dominant edible mushroom cultivated on wood. The major xylanase detected in cultures grown on a commercial oak wood medium was extracted, purified, and characterized. The enzyme was a non-debranching endo- beta -D-xylanase (1,4- beta -D-xylan xylanohydrolase; E.C.3.2.1.8) highly specific for xylans, with a molecular weight of 41,000 (on sodium dodecyl sulfate gels) and an isoelectric point of 3.6. With aspen glucuronoxylan as substrate, the enzyme showed optimal activity at pH 4.5-5.0 and 60 degree C, with a K sub(m) of 0.66 mg/ml and specific activity of 310 units/mg protein at 40 degree C. It was capable of hydrolyzing (forming reducing sugars from) 40%-50% of the hydrolyzable linkages in either glucuronoxylan or arabinoxylan. The enzyme produced xylose and major identifiable products in the xylobiose or xylotriose (and presumably larger) size range. |
doi_str_mv | 10.1007/BF00176530 |
format | article |
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T ; KELLEY, B. D ; BURGESS, R. R ; LEATHAM, G. F</creator><creatorcontrib>MISHRA, C ; FORRESTER, I. T ; KELLEY, B. D ; BURGESS, R. R ; LEATHAM, G. F</creatorcontrib><description>The white-rot basidiomycete Lentinula (syn. Lentinus) edodes (Berk.) Pegler is the dominant edible mushroom cultivated on wood. The major xylanase detected in cultures grown on a commercial oak wood medium was extracted, purified, and characterized. The enzyme was a non-debranching endo- beta -D-xylanase (1,4- beta -D-xylan xylanohydrolase; E.C.3.2.1.8) highly specific for xylans, with a molecular weight of 41,000 (on sodium dodecyl sulfate gels) and an isoelectric point of 3.6. With aspen glucuronoxylan as substrate, the enzyme showed optimal activity at pH 4.5-5.0 and 60 degree C, with a K sub(m) of 0.66 mg/ml and specific activity of 310 units/mg protein at 40 degree C. It was capable of hydrolyzing (forming reducing sugars from) 40%-50% of the hydrolyzable linkages in either glucuronoxylan or arabinoxylan. The enzyme produced xylose and major identifiable products in the xylobiose or xylotriose (and presumably larger) size range.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/BF00176530</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin: Springer</publisher><subject>arabinoxylan ; Biological and medical sciences ; Biotechnology ; endo-1,4- beta -xylanase ; Enzyme engineering ; Fundamental and applied biological sciences. Psychology ; glucuronoxylan ; hydrolysis ; Improved methods for extraction and purification of enzymes ; Methods. Procedures. 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F</creatorcontrib><title>Characterization of a major xylanase purified from Lentinula edodes cultures grown on a commercial solid lignocellulosic substrate</title><title>Applied microbiology and biotechnology</title><description>The white-rot basidiomycete Lentinula (syn. Lentinus) edodes (Berk.) Pegler is the dominant edible mushroom cultivated on wood. The major xylanase detected in cultures grown on a commercial oak wood medium was extracted, purified, and characterized. The enzyme was a non-debranching endo- beta -D-xylanase (1,4- beta -D-xylan xylanohydrolase; E.C.3.2.1.8) highly specific for xylans, with a molecular weight of 41,000 (on sodium dodecyl sulfate gels) and an isoelectric point of 3.6. With aspen glucuronoxylan as substrate, the enzyme showed optimal activity at pH 4.5-5.0 and 60 degree C, with a K sub(m) of 0.66 mg/ml and specific activity of 310 units/mg protein at 40 degree C. It was capable of hydrolyzing (forming reducing sugars from) 40%-50% of the hydrolyzable linkages in either glucuronoxylan or arabinoxylan. The enzyme produced xylose and major identifiable products in the xylobiose or xylotriose (and presumably larger) size range.</description><subject>arabinoxylan</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>endo-1,4- beta -xylanase</subject><subject>Enzyme engineering</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>glucuronoxylan</subject><subject>hydrolysis</subject><subject>Improved methods for extraction and purification of enzymes</subject><subject>Methods. Procedures. 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F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c326t-8bd06d11b8339dcd3994d1d5bae378b8d54a5eed548be602d76b3472b8e46223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>arabinoxylan</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>endo-1,4- beta -xylanase</topic><topic>Enzyme engineering</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>glucuronoxylan</topic><topic>hydrolysis</topic><topic>Improved methods for extraction and purification of enzymes</topic><topic>Methods. Procedures. Technologies</topic><topic>xylooligosaccharides</topic><topic>xylose</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MISHRA, C</creatorcontrib><creatorcontrib>FORRESTER, I. T</creatorcontrib><creatorcontrib>KELLEY, B. D</creatorcontrib><creatorcontrib>BURGESS, R. 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F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a major xylanase purified from Lentinula edodes cultures grown on a commercial solid lignocellulosic substrate</atitle><jtitle>Applied microbiology and biotechnology</jtitle><date>1990-05-01</date><risdate>1990</risdate><volume>33</volume><issue>2</issue><spage>226</spage><epage>232</epage><pages>226-232</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><abstract>The white-rot basidiomycete Lentinula (syn. Lentinus) edodes (Berk.) Pegler is the dominant edible mushroom cultivated on wood. The major xylanase detected in cultures grown on a commercial oak wood medium was extracted, purified, and characterized. The enzyme was a non-debranching endo- beta -D-xylanase (1,4- beta -D-xylan xylanohydrolase; E.C.3.2.1.8) highly specific for xylans, with a molecular weight of 41,000 (on sodium dodecyl sulfate gels) and an isoelectric point of 3.6. With aspen glucuronoxylan as substrate, the enzyme showed optimal activity at pH 4.5-5.0 and 60 degree C, with a K sub(m) of 0.66 mg/ml and specific activity of 310 units/mg protein at 40 degree C. It was capable of hydrolyzing (forming reducing sugars from) 40%-50% of the hydrolyzable linkages in either glucuronoxylan or arabinoxylan. The enzyme produced xylose and major identifiable products in the xylobiose or xylotriose (and presumably larger) size range.</abstract><cop>Berlin</cop><pub>Springer</pub><doi>10.1007/BF00176530</doi><tpages>7</tpages></addata></record> |
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subjects | arabinoxylan Biological and medical sciences Biotechnology endo-1,4- beta -xylanase Enzyme engineering Fundamental and applied biological sciences. Psychology glucuronoxylan hydrolysis Improved methods for extraction and purification of enzymes Methods. Procedures. Technologies xylooligosaccharides xylose |
title | Characterization of a major xylanase purified from Lentinula edodes cultures grown on a commercial solid lignocellulosic substrate |
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