Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/12632
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dc.contributorDepartment of Applied Biology and Chemical Technology-
dc.creatorHuang, H-
dc.creatorKwok, KC-
dc.creatorLiang, HH-
dc.date.accessioned2015-07-14T01:27:13Z-
dc.date.available2015-07-14T01:27:13Z-
dc.identifier.issn1350-4177-
dc.identifier.urihttp://hdl.handle.net/10397/12632-
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.rights© 2007 Elsevier B.V.en_US
dc.rightsThis is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/)en_US
dc.rightsThe following publication Huang, H., Kwok, K. C., & Liang, H. H. (2008). Inhibitory activity and conformation changes of soybean trypsin inhibitors induced by ultrasound. Ultrasonics sonochemistry, 15(5), 724-730 is available at https://doi.org/10.1016/j.ultsonch.2007.10.007en_US
dc.subjectConformationen_US
dc.subjectInhibitory activityen_US
dc.subjectTrypsin inhibitoren_US
dc.subjectUltrasounden_US
dc.titleInhibitory activity and conformation changes of soybean trypsin inhibitors induced by ultrasounden_US
dc.typeJournal/Magazine Articleen_US
dc.identifier.spage724-
dc.identifier.epage730-
dc.identifier.volume15-
dc.identifier.issue5-
dc.identifier.doi10.1016/j.ultsonch.2007.10.007-
dcterms.abstractThe inhibitory activities, sulfhydryl bonds and far-UV circular dichroism (CD) spectra of Kunitz and Bowman-Birk soybean trypsin inhibitors (KTI and BBTI) were measured before and after ultrasound treatments. The differences between KTI and BBTI in conformation changes and resistance to ultrasound were observed. The secondary structures of KTI were found to be composed of β-sheet (22.5%), β-turn (16.2%) and random coils (61.4%) while that of BBTI composed of only β-sheet (52.6%) and random coils (47.4%). KTI lost its inhibitory activity more quickly than BBTI, proportionally to the ultrasound amplitudes and sonication durations used. Relevant synchronous phenomena observed included the inactivation of KTI, significant rise in sulfhydryl content and corresponding conformation changes, in which there were dramatic decreases in both β-turn and random coil contents and increase in the β-sheet structure over the entire sonication duration and ultrasonic amplitude scale used by the study. Ultrasound affected the activities and conformations of KTI and BBTI by exerting an influence on their disulfide bonds. For KTI, up to 55% of inhibitory activity could be inactivated, at which about 71.5% of disulfide bonds were altered and the [θ]200nm value was changed from native -2545 deg cm2 dmol-1 to -1827 deg cm2 dmol-1. Whereas for BBTI, far-UV CD spectra, β-sheet and random structures were barely affected, only about 5.29% of disulfide bonds were found altered and the [θ]200nm value was changed only from native -797 deg cm2 dmol-1 to -700 deg cm2 dmol-1. It is concluded that ultrasound inactivates KTI by inducing a reduction in the disulfide bonds and then changes the conformations.-
dcterms.accessRightsopen accessen_US
dcterms.bibliographicCitationUltrasonics sonochemistry, 2008, v. 15, no. 5, p. 724-730-
dcterms.isPartOfUltrasonics sonochemistry-
dcterms.issued2008-
dc.identifier.isiWOS:000255901700012-
dc.identifier.scopus2-s2.0-41549145917-
dc.identifier.pmid18082441-
dc.identifier.rosgroupidr43745-
dc.description.ros2008-2009 > Academic research: refereed > Publication in refereed journal-
dc.description.oaVersion of Recorden_US
dc.identifier.FolderNumberOA_IR/PIRAen_US
dc.description.pubStatusPublisheden_US
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