Inactivation of lysozyme by ultrasonic waves under pressure at different temperatures

Mañas, Pilar; Muñoz, Benito; Sanz, David López; Condón, S.

doi:10.1016/j.enzmictec.2005.11.053

Cited by 45 publications

(23 citation statements)

References 17 publications

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“…It is thought that sonication produces haemolytic water molecule cleavage, generating high energy intermediates such as hydroxyl and hydrogen free radicals, and therefore, causing protein structural changes (Barteri, Diociaiuti, Pala, & Rotella, 2004;Gulseren, Guzey, Bruce, & Weiss, 2007). It was reported (Manas, Munoz, Sanz, & Condon, 2006) that lysozyme activity was significantly decreased under sonication at 80°C for up to 15 min along with a significant lose of the disulphide bonds and a significant increase of the reactive SH groups. Similar to our results, Huang, Kwok, and Liang (2008) reported that the sulphydryl group content of Bowman-Birk trypsin inhibitor (BBTI) was not affected during the first 5 min sonication, but that of Kunitz trypsin inhibitor (KTI) was increased linearly with the time of the sonication at 20 kHz.…”

Section: Effect Of Sonication On the Sulphydryl Groupsmentioning

confidence: 97%

Effect of sonication on thermolysin hydrolysis of ovotransferrin

et al. 2011

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Section: Effect Of Sonication On the Sulphydryl Groupsmentioning

confidence: 97%

Effect of sonication on thermolysin hydrolysis of ovotransferrin

et al. 2011

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“…Protease 3 produced by Pseudomonas fluorescens was resistant to manothermosonication (ultrasound combined with heat and pressure) at 30°C but was very sensitive at 76°C (Vercet et al, 2002). Manas et al (2006) reported that ultrasonication (117 µm) at room temperature and atmospheric pressure had no effect on lysozyme activity, whereas applying 200 kPa pressure and increasing temperature to between 60 and 80°C increased the inactivation rate; the power value was not reported. A synergistic effect is observed when heat is combined with ultrasound (Lopez et al, 1994;Villamiel and de Jong, 2000b;Vercet et al, 2002), and this opens the door for many applications in the food industry, particularly in enzyme inactivation.…”

Section: Introductionmentioning

confidence: 95%

Quality characteristics and plasmin activity of thermosonicated skim milk and cream

Vijayakumar

Grewell

Annandarajah

et al. 2015

Journal of Dairy Science

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The shelf life of pasteurized milk is limited by heat-stable proteases, which cause gelation and bitter taste upon extended storage of milk. Ultra-high temperature processing inactivates proteases but detrimentally affects milk's sensory quality. An adjunct to pasteurization is desired to extend milk's shelf life while maintaining quality characteristics. In this study, the effects of combined heat and ultrasound (thermosonication) on total plasmin activity and various quality characteristics of skim milk and cream were studied. Thermosonication, at an average power of 115 W (152 µmp-p, where p-p=peak-to-peak amplitude) for 3 min, decreased the total plasmin activity (i.e., plasmin- and plasminogen-derived activity) by nearly 94% in fresh skim milk and cream. Enzyme activity in thermosonicated skim milk samples measured at the end of 30 d was 5- to 10-fold higher than on d 0, but remained stable in thermosonicated cream. Descriptive analysis of odor attributes was conducted for up to 4 wk with 8 trained panelists. No significant differences were observed between the intensities of offensive "eggy" and "rubbery" odor attributes of thermosonicated skim milk and pasteurized commercial skim milk and cream. In addition, lightness (L*) values and viscosity were not adversely affected by thermosonication. Thermosonication decreased the fat globule size in skim milk and cream, and the homogenizing effect increased with treatment time. Thermosonication at average powers of 104 W (133 µmp-p) and 115 W (152 µmp-p) for 1 and 3 min destroyed coliforms and over 99% of the total aerobic bacteria. The total aerobic bacteria counts of thermosonicated skim milk and cream samples were less than 20,000 cfu/mL on d 30. Because thermosonication did not induce off-aromas or viscosity changes but did inactivate microorganisms and protease enzymes, thermosonication may be an appropriate adjunct to pasteurization to extend milk shelf life.

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“…Under these extreme changes, hydrogen bonds and van der Waals bonding in the enzyme structure can be broken down, which results in the loss of enzyme activity (Zhong et al, 2004). Additionally, chemical effects are due to free radical mediated inactivation observed in many cases (Barteri et al, 2004;Basto et al, 2007;Raviyan et al, 2005;Manas et al, 2006;Terefe et al, 2009Terefe et al, , 2015. The formation of high energy free radicals due to sonication could lead to sonolysis of water molecules.…”

Section: Introductionmentioning

confidence: 98%

“…The enzyme inactivation is mainly due to mechanical and chemical effects (Barteri et al, 2004;Basto et al, 2007;Raviyan et al, 2005;Manas et al, 2006;Terefe et al, 2009Terefe et al, , 2015. The cavitation caused by the formation and collapsing of micro-size bubbles releases huge amounts of energy, which is claimed to increase the temperature (up to 5000 K) and pressure (50 MPa) at a micro scale.…”

Section: Introductionmentioning

confidence: 99%