Characterizaiton of cold-and high-pressure-active polygalacturonases from a deep-sea yeast, Cryptococcus liquefaciens strain N6

A deep-sea yeast, Cryptococcus liquefaciens strain N6, produces two polygalacturonases, p36 and p40 (N6PGases). These N6-PGases were highly active at 0-10 deg C in comparison to a PGase from Aspergillus japonicus. The hydrolytic activity of these N6-PGases remained almost unchanged up to a hydrostat...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2006-01, Vol.70 (1)
Hauptverfasser:	Abe, F.(Japan Agency for Marine-Earth Science and Technology, Yokosuka, Kanagawa), Minegishi, H, Miura, T, Nagahama, T, Usami, R, Horikoshi, K
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Sprache:	eng
Schlagworte:	CHEMICAL REACTIONS CRYPTOCOCCUS (CHAMPIGNON) CRYPTOCOCCUS (FUNGI) CRYPTOCOCCUS (HONGO) ENZYMATIC HYDROLYSIS FRUIT JUICES HIDROLISIS ENZIMATICA HIGH PRESSURE TECHNOLOGY HYDROLYSE ENZYMATIQUE JUGO DE FRUTAS JUS DE FRUITS LEVADURA LEVURE POLIGALACTURONASA POLYGALACTURONASE REACCIONES QUIMICAS REACTION CHIMIQUE TECHNOLOGIE HAUTE PRESSION TECNOLOGIA ALTA PRESION YEASTS
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creator	Abe, F.(Japan Agency for Marine-Earth Science and Technology, Yokosuka, Kanagawa) Minegishi, H Miura, T Nagahama, T Usami, R Horikoshi, K
description	A deep-sea yeast, Cryptococcus liquefaciens strain N6, produces two polygalacturonases, p36 and p40 (N6PGases). These N6-PGases were highly active at 0-10 deg C in comparison to a PGase from Aspergillus japonicus. The hydrolytic activity of these N6-PGases remained almost unchanged up to a hydrostatic pressure of 100MPa at 24 deg C with a very small activation volume of -1.1ml/mol. At 10 deg C, however, the activation volume increased to 3.3 or 5.4 ml/mol (p36 and p40, respectively), suggesting that the enzyme-substrate complexes can expand at their transition states. We speculate that such a volume expansion upon forming the enzyme substrate complexes contributes to decreasing the activation energy for hydrolysis. This can account for the high activity of N6-PGases at lowtemperature.
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These N6-PGases were highly active at 0-10 deg C in comparison to a PGase from Aspergillus japonicus. The hydrolytic activity of these N6-PGases remained almost unchanged up to a hydrostatic pressure of 100MPa at 24 deg C with a very small activation volume of -1.1ml/mol. At 10 deg C, however, the activation volume increased to 3.3 or 5.4 ml/mol (p36 and p40, respectively), suggesting that the enzyme-substrate complexes can expand at their transition states. We speculate that such a volume expansion upon forming the enzyme substrate complexes contributes to decreasing the activation energy for hydrolysis. This can account for the high activity of N6-PGases at lowtemperature.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><language>eng</language><subject>CHEMICAL REACTIONS ; CRYPTOCOCCUS (CHAMPIGNON) ; CRYPTOCOCCUS (FUNGI) ; CRYPTOCOCCUS (HONGO) ; ENZYMATIC HYDROLYSIS ; FRUIT JUICES ; HIDROLISIS ENZIMATICA ; HIGH PRESSURE TECHNOLOGY ; HYDROLYSE ENZYMATIQUE ; JUGO DE FRUTAS ; JUS DE FRUITS ; LEVADURA ; LEVURE ; POLIGALACTURONASA ; POLYGALACTURONASE ; REACCIONES QUIMICAS ; REACTION CHIMIQUE ; TECHNOLOGIE HAUTE PRESSION ; TECNOLOGIA ALTA PRESION ; YEASTS</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2006-01, Vol.70 (1)</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids></links><search><creatorcontrib>Abe, F.(Japan Agency for Marine-Earth Science and Technology, Yokosuka, Kanagawa)</creatorcontrib><creatorcontrib>Minegishi, H</creatorcontrib><creatorcontrib>Miura, T</creatorcontrib><creatorcontrib>Nagahama, T</creatorcontrib><creatorcontrib>Usami, R</creatorcontrib><creatorcontrib>Horikoshi, K</creatorcontrib><title>Characterizaiton of cold-and high-pressure-active polygalacturonases from a deep-sea yeast, Cryptococcus liquefaciens strain N6</title><title>Bioscience, biotechnology, and biochemistry</title><description>A deep-sea yeast, Cryptococcus liquefaciens strain N6, produces two polygalacturonases, p36 and p40 (N6PGases). These N6-PGases were highly active at 0-10 deg C in comparison to a PGase from Aspergillus japonicus. The hydrolytic activity of these N6-PGases remained almost unchanged up to a hydrostatic pressure of 100MPa at 24 deg C with a very small activation volume of -1.1ml/mol. At 10 deg C, however, the activation volume increased to 3.3 or 5.4 ml/mol (p36 and p40, respectively), suggesting that the enzyme-substrate complexes can expand at their transition states. We speculate that such a volume expansion upon forming the enzyme substrate complexes contributes to decreasing the activation energy for hydrolysis. 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These N6-PGases were highly active at 0-10 deg C in comparison to a PGase from Aspergillus japonicus. The hydrolytic activity of these N6-PGases remained almost unchanged up to a hydrostatic pressure of 100MPa at 24 deg C with a very small activation volume of -1.1ml/mol. At 10 deg C, however, the activation volume increased to 3.3 or 5.4 ml/mol (p36 and p40, respectively), suggesting that the enzyme-substrate complexes can expand at their transition states. We speculate that such a volume expansion upon forming the enzyme substrate complexes contributes to decreasing the activation energy for hydrolysis. This can account for the high activity of N6-PGases at lowtemperature.</abstract></addata></record>
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source	J-STAGE Free; Oxford University Press Journals All Titles (1996-Current); Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry
subjects	CHEMICAL REACTIONS CRYPTOCOCCUS (CHAMPIGNON) CRYPTOCOCCUS (FUNGI) CRYPTOCOCCUS (HONGO) ENZYMATIC HYDROLYSIS FRUIT JUICES HIDROLISIS ENZIMATICA HIGH PRESSURE TECHNOLOGY HYDROLYSE ENZYMATIQUE JUGO DE FRUTAS JUS DE FRUITS LEVADURA LEVURE POLIGALACTURONASA POLYGALACTURONASE REACCIONES QUIMICAS REACTION CHIMIQUE TECHNOLOGIE HAUTE PRESSION TECNOLOGIA ALTA PRESION YEASTS
title	Characterizaiton of cold-and high-pressure-active polygalacturonases from a deep-sea yeast, Cryptococcus liquefaciens strain N6
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