2000
DOI: 10.1016/s0032-9592(00)00141-2
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The stability of enzymes after sonication

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Cited by 158 publications
(58 citation statements)
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“…Such as, Villamiel and de Jong [47] reported that ultrasound treatment (20 kHz, 120 μm) at temperature less than 55˚C did not inactivate alkaline phosphatase in milk, while only 22 and 14% inactivation was observed in γ-glutamyltranspeptidase and lactoperoxidase, respectively. Similar results were obtained for sonication (20 kHz, 7 -40 W) of alkaline phosphatase in buffer [41].…”
Section: Enzyme Inactivationsupporting
confidence: 84%
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“…Such as, Villamiel and de Jong [47] reported that ultrasound treatment (20 kHz, 120 μm) at temperature less than 55˚C did not inactivate alkaline phosphatase in milk, while only 22 and 14% inactivation was observed in γ-glutamyltranspeptidase and lactoperoxidase, respectively. Similar results were obtained for sonication (20 kHz, 7 -40 W) of alkaline phosphatase in buffer [41].…”
Section: Enzyme Inactivationsupporting
confidence: 84%
“…Enzyme inactivation generally increases with increasing ultrasound power, ultrasound freqency, exposure time, amplitude level, cavitation intensity, processing temperature and processing pressure, but decreases as the volume being treated increases [34,35,41,46].…”
Section: Enzyme Inactivationmentioning
confidence: 99%
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“…These aggregates are produced by the exposure of the cystine residues in proteins to the superoxide radicals which are formed during sonication; this causes the formation of disulphide bonds between proteins [38]. However, an intermittent ultrasonic treatment using a duty cycle (as used in this study) could reduce the formation of free radicals [39]. There was no significant decrease in laccase after 5 min of sonication for the cellfree supernatants after 48 and 60 h of the cultivation (data not shown).…”
Section: Effect Of the Ultrasonic Treatment On The Release Of Intracementioning
confidence: 95%