Effect of atmospheric pressure cold plasma (ACP) on activity and structure of alkaline phosphatase

被引:91
作者
Segat, Annalisa [1 ,2 ]
Misra, N. N. [2 ,3 ]
Cullen, P. J. [2 ,4 ]
Innocente, Nadia [1 ]
机构
[1] Univ Udine, Dept Agr Food Environm & Anim Sci, Via Sondrio,2-A, I-33100 Udine, Italy
[2] Dublin Inst Technol, Sch Food Sci & Environm Hlth, Dublin, Ireland
[3] Gen Mills IPL, Res & Dev, GTECH, Mumbai, Maharashtra, India
[4] Univ New S Wales, Sch Chem Engn, Sydney, NSW, Australia
关键词
Alkaline phosphatase; Cold plasma; Enzyme; Circular dichroism; Spectroscopy; Chemometrics; PULSED ELECTRIC-FIELDS; CIRCULAR-DICHROISM; INACTIVATION; SECONDARY; PROTEINS; PACKAGE; MILK; TEMPERATURE; MECHANISM; DEGRADATION;
D O I
10.1016/j.fbp.2016.01.010
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Atmospheric cold plasma treatments (ACP) is a novel non-thermal processing technology with several emerging potential applications in food processing, including dairy. This study evaluates the effect of ACP on the activity and structure of alkaline phosphatase (ALP), an enzyme native to milk. ALP enzyme in solution was treated with ACP at three discreet high voltages (40, 50 and 60 kV) for durations ranging between 15 s and 5 min. Results demonstrated that the dielectric barrier discharge based plasma technology was able to inactivate the enzyme within a few seconds. Kinetic models, namely first order, Weibull and logistic models were fitted to the experimentally observed data and the model parameters were determined. The Weibull model was found to best describe the observed variance in residual activity for all the voltages applied. The dichroic spectra suggested that the enzyme was characterized by a predominance of alpha-helix structure, and the helical content showed a tendency to decrease with increase in treatment time and voltage. The maximum temperature recorded for most intense treatments was in the order of only 30 degrees C and no change in pH was noticed. (C) 2016 The Institution of Chemical Engineers. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:181 / 188
页数:8
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