Enzymatic proteolysis and in situ digestion as strategies to determine Cs and Sr in fish by tungsten coil atomic emission spectrometry

Santos, LN; Donati, GL; Calloway, CP, Jr; Jones, BT; Nobrega, JA

HERO ID

1565970

Reference Type

Journal Article

Year

2012

HERO ID 1565970
In Press No
Year 2012
Title Enzymatic proteolysis and in situ digestion as strategies to determine Cs and Sr in fish by tungsten coil atomic emission spectrometry
Authors Santos, LN; Donati, GL; Calloway, CP, Jr; Jones, BT; Nobrega, JA
Journal Journal of Analytical Atomic Spectrometry
Volume 27
Issue 12
Page Numbers 2082-2087
Abstract Papain is employed to pre-digest and homogenize fish slurries which are directly placed on a tungsten coil atomizer and digested in situ with an oxidizing mixture of HNO3 and H2O2. Both Cs and Sr are determined in different fish samples by tungsten coil atomic emission spectrometry (WCAES) with limits of detection of 0.07 and 0.15 mu g l(-1), respectively. Sample aliquots of 50 mu l are dried, digested/pyrolyzed and atomized using a 400 W miniature solid-state constant current power supply and a Visual Basic temperature control program. The portable WCAES instrumental setup is composed of a small metallic atomization cell, a 2.54 cm diameter fused silica lens and a hand-held charge coupled device-based spectrometer. Tungsten filaments extracted from 24 V, 250 W commercially available light bulbs are used as atomizers. The method accuracy is demonstrated by comparing WCAES results with values obtained by ICP OES. No statistically significant differences are observed between the results from each different method at a 95% confidence level. Recovery tests are also carried out for Cs and values between 100 and 110% are obtained. The method precision is calculated to be 6.8 and 7.3% for 2.5 mu g l(-1) of Cs and 100 mu g l(-1) of Sr (n = 10), respectively. The method described is simple, fast and efficient, offering an interesting alternative for applications in food safety control and determinations in the field.
Doi 10.1039/c2ja30146f
Wosid WOS:000310855000005
Is Certified Translation No
Dupe Override No
Comments Source: Web of Science WOS:000310855000005
Is Public Yes