Multi-Sensing Techniques with Ultrasound for Musculoskeletal Assessment: A Review.

The study of muscle contractions generated by the muscle-tendon unit (MTU) plays a critical role in medical diagnoses, monitoring, rehabilitation, and functional assessments, including the potential for movement prediction modeling used for prosthetic control. Over the last decade, the use of combined traditional techniques to quantify information about the muscle condition that is correlated to neuromuscular electrical activation and the generation of muscle force and vibration has grown. The purpose of this review is to guide the reader to relevant works in different applications of ultrasound imaging in combination with other techniques for the characterization of biological signals. Several research groups have been using multi-sensing systems to carry out specific studies in the health area. We can divide these studies into two categories: human-machine interface (HMI), in which sensors are used to capture critical information to control computerized prostheses and/or robotic actuators, and physiological study, where sensors are used to investigate a hypothesis and/or a clinical diagnosis. In addition, the relevance, challenges, and expectations for future work are discussed.

High-power therapeutic ultrasound for treatment of abdominal localized adiposity-double-blind randomized clinical trial.

This study aimed to evaluate the effects of high-power therapeutic ultrasound in the treatment of abdominal localized adiposity in an isolated manner, with the use of neutral gel comparing ultrasonic application with 5% lipolytic active caffeine gel (phonophoresis). A total of 90 healthy women aged between 18 and 40 years were randomized and divided into two groups. The volunteers underwent anamnesis evaluation, perimetry, bioimpedance, ultrasound examination, and blood tests (complete lipidogram, creatinine, and vitamin D) before and after the end of the 10-session ultrasound protocol (3 MHz, 2 W/cm2, and 30w). Comparisons between groups and pre-post evaluation were performed by a two-way repeated-measures analysis of variance. Values of p < 0.05 indicated statistical significance. The results demonstrated a significant reduction in both groups, for the perimetry (p < 0.001) and measurements of adipose tissue thickness (p < 0.001). The examinations exhibited a significant alteration only of the complete lipidogram, but without significance (p > 0.05). When comparing the groups, no statistically significant difference was identified in any of the analyzed parameters. The high-power ultrasonic therapy is efficient in reducing localized adiposity, regardless of whether it is applied with neutral gel or 5% caffeine gel.

Image reconstruction utilizing median filtering applied to elastography.

BACKGROUND: The resources of ultrafast technology can be used to add another analysis to ultrasound imaging: assessment of tissue viscoelasticity. Ultrafast image formation can be utilized to find transitory shear waves propagating in soft tissue, which permits quantification of the mechanical properties of the tissue via elastography. This technique permits simple and noninvasive diagnosis and monitoring of disease. METHODS: This article presents a method to estimate the viscoelastic properties and rigidity of structures using the ultrasound technique known as shear wave elasticity imaging (SWEI). The Verasonics Vantage 128 research platform and L11-4v transducer were used to acquire radio frequency signals from a model 049A elastography phantom (CIRS, USA), with subsequent processing and analysis in MATLAB. RESULTS: The images and indexes obtained reflect the qualitative measurements of the different regions of inclusions in the phantom and the respective alterations in the viscoelastic properties of distinct areas. Comparison of the results obtained with this proposed technique and other commonly used techniques demonstrates the characteristics of median filtering in smoothing variations in velocity to form elastographic images. The results from the technique proposed in this study are within the margins of error indicated by the phantom manufacturer for each type of inclusion; for the phantom base and for type I, II, III, and IV inclusions, respectively, in kPa and percentage errors, these are 25 (24.0%), 8 (37.5%), 14 (28.6%), 45 (17.8%), and 80 (15.0%). The values obtained using the method proposed in this study and mean percentage errors were 29.18 (- 16.7%), 10.26 (- 28.2%), 15.64 (- 11.7%), 45.81 (- 1.8%), and 85.21 (- 6.5%), respectively. CONCLUSIONS: The new technique to obtain images uses a distinct filtering function which considers the mean velocity in the region around each pixel, in turn allowing adjustments according to the characteristics of the phantom inclusions within the ultrasound and optimizing the resulting elastographic images.

Eigenspace generalized sidelobe canceller combined with SNR dependent coherence factor for plane wave imaging.

BACKGROUND: The eigenspace generalized sidelobe canceller (EGSC) beamformer combined with a signal-to-noise ratio (SNR) dependent coherence factor (CF) is suggested for coherent plane wave compounding (PW) imaging. Conventional CF based methods such as generalized CF and subarray CF can improve the image quality, however, they are not suitable for low SNR. On the other hand, the EGSC CF based approach can introduce improvements in image quality, however, in PW imaging is susceptible to suffer from degradation due to low SNR which leads to a poor image quality. To overcome this limitation, the SNR dependent CF method is suggested for application in such situations due to its ability to control the SNR levels. METHODS: The Field II and the Verasonics ultrasound imaging system with a L11-4v array transducer with a contrast resolution phantom were used to capture the plane wave sequences of simulation and experimental data, respectively. The performance evaluation using full width at half maximum (FWHM), contrast (CR and CNR) and the speckle statistics by using the signal to noise ratio (SNR) complemented by the Rayleigh distribution analysis was performed. In order to evaluate the performance of the [Formula: see text] (the SNR CF) beamformer, the comparison is done with particular importance to other CF-based approaches such as [Formula: see text] (the generalized CF) and, [Formula: see text] (the subarray CF) respectively. RESULTS: Taking DAS as reference, [Formula: see text] showed 30.3 and 39.5% of improvement for [Formula: see text] and [Formula: see text], respectively, when using experimental data. The proposed method also slightly outperforms the [Formula: see text] and [Formula: see text] methods for [Formula: see text], [Formula: see text], and speckle statistics assessment. CONCLUSION: The [Formula: see text] is, therefore, suitable for CPWC by improving the spatial resolution and contrast while preserving the speckle pattern.

Polystyrene Oxygen Optodes Doped with Ir(III) and Pd(II) meso-Tetrakis(pentafluorophenyl)porphyrin Using an LED-Based High-Sensitivity Phosphorimeter.

This paper presents a gaseous oxygen detection system based on time-resolved phosphorimetry (time-domain), which is used to investigate O2 optical transducers. The primary sensing elements were formed by incorporating iridium(III) and palladium(II) meso-tetrakis(pentafluorophenyl)porphyrin complexes (IrTFPP-CO-Cl and PdTFPP) in polystyrene (PS) solid matrices. Probe excitation was obtained using a violet light-emitting diode (LED) (low power), and the resulting phosphorescence was detected by a high-sensitivity compact photomultiplier tube. The detection system performance and the preparation of the transducers are presented along with their optical properties, phosphorescence lifetimes, calibration curves and photostability. The developed lifetime measuring system showed a good signal-to-noise ratio, and reliable results were obtained from the optodes, even when exposed to moderate levels of O2. The new IrTFPP-CO-Cl membranes exhibited room temperature phosphorescence and moderate sensitivity: <τ0>/<τ21%> ratio of ≈6. A typically high degree of dynamic phosphorescence quenching was observed for the traditional indicator PdTFPP: <τ0>/<τ21%> ratio of ≈36. Pulsed-source time-resolved phosphorimetry combined with a high-sensitivity photodetector can offer potential advantages such as: (i) major dynamic range, (ii) extended temporal resolution (Δτ/Δ[O2]) and (iii) high operational stability. IrTFPP-CO-Cl immobilized in polystyrene is a promising alternative for O2 detection, offering adequate photostability and potentially mid-range sensitivity over Pt(II) and Pd(II) metalloporphyrins.

Generation and Analysis of Ultrasound Images Using Plane Wave and Sparse Arrays Techniques.

Ultrasonic imaging is one of the most important techniques to help medical diagnosis. However, obtaining high quality images requires the acquisition, processing, and storage of a large amount of data. In this work, we evaluated a new ultrasound imaging technique based on plane wave and sparse arrays to increase the scan rate and reduce the amount of data amount to be stored. The performance of the proposed method was tested using simulated echo data (from Field II) and phantom data acquired using a Verasonics system equipped with a L11-4v linear array transducer. The tests were done using 128 elements for transmission and 128, 65, 44, and 23 elements sparsely distributed for reception. The simulated data were compared with images obtained with the Delay and Sum (DAS) method and the experimental data were compared with those acquired from Verasonics. The obtained results using the Full Width at Half Maximum (FWHM) criteria at -6 dB showed that the images generated by the proposed method were similar in terms of resolutions (axial and lateral) and contrast to the simulated and the Verasonics commercial ones, indicating that the sparse reception proposed method is suitable for ultrasound imaging.

An Assessment of Iterative Reconstruction Methods for Sparse Ultrasound Imaging.

Ultrasonic image reconstruction using inverse problems has recently appeared as an alternative to enhance ultrasound imaging over beamforming methods. This approach depends on the accuracy of the acquisition model used to represent transducers, reflectivity, and medium physics. Iterative methods, well known in general sparse signal reconstruction, are also suited for imaging. In this paper, a discrete acquisition model is assessed by solving a linear system of equations by an ℓ 1 -regularized least-squares minimization, where the solution sparsity may be adjusted as desired. The paper surveys 11 variants of four well-known algorithms for sparse reconstruction, and assesses their optimization parameters with the goal of finding the best approach for iterative ultrasound imaging. The strategy for the model evaluation consists of using two distinct datasets. We first generate data from a synthetic phantom that mimics real targets inside a professional ultrasound phantom device. This dataset is contaminated with Gaussian noise with an estimated SNR, and all methods are assessed by their resulting images and performances. The model and methods are then assessed with real data collected by a research ultrasound platform when scanning the same phantom device, and results are compared with beamforming. A distinct real dataset is finally used to further validate the proposed modeling. Although high computational effort is required by iterative methods, results show that the discrete model may lead to images closer to ground-truth than traditional beamforming. However, computing capabilities of current platforms need to evolve before frame rates currently delivered by ultrasound equipments are achievable.

A reconfigurable arbitrary waveform generator using PWM modulation for ultrasound research.

BACKGROUND: In ultrasound imaging systems, the digital transmit beamformer is a critical module that generates accurate control over several transmission parameters. However, such transmit front-end module is not typically accessible to ultrasound researchers. To overcome this difficulty, we have been developing a compact and fully programmable digital transmit system using the pulse-width modulation (PWM) technique for generating simultaneous arbitrary waveforms, specifically designed for research purposes. METHODS: In this paper we present a reconfigurable arbitrary waveform generator (RAWG) for ultrasound research applications that exploits a high frequency PWM scheme implemented in a low-cost FPGA, taking advantage of its flexibility and parallel processing capability for independent controlling of multiple transmission parameters. The 8-channel platform consists of a FPGA-based development board including an USB 2.0 interface and an arbitrary waveform generator board with eight MD2130 beamformer source drivers for individual control of waveform, amplitude apodization, phase angle and time delay trigger. RESULTS: To evaluate the efficiency of our system, we used equivalent RC loads (1 kΩ and 220 pF) to produce arbitrary excitation waveforms with the Gaussian and Tukey profiles. The PWM carrier frequency was set at 160 MHz featuring high resolution while keeping a minimum time delay of 3.125 ns between pulses to enable the acoustic beam to be focused and/or steered electronically. Preliminary experimental results show that the RAWG can produce complex arbitrary pulses with amplitude over 100 Vpp and central frequency up to 20 MHz with satisfactory linearity of the amplitude apodization, as well as focusing phase adjustment capability with angular resolution of 7.5°. CONCLUSIONS: The initial results of this study showed that the proposed research system is suitable for generating simultaneous arbitrary waveforms, providing extensive user control with direct digital access to the various transmission parameters needed to explore alternative ultrasound transmission techniques.

Safety evaluation of the food enzyme phospholipase A2 from the genetically modified Streptomyces violaceoruber strain AS-10.

The food enzyme phospholipase A2 (phosphatidylcholine 2-acylhydrolase EC 3.1.1.4) is produced with the genetically modified Streptomyces violaceoruber strain AS-10 by Nagase (Europa) GmbH. The genetic modifications do not give rise to safety concerns. The food enzyme is free from viable cells of the production organism and its DNA. It is intended to be used in four food manufacturing processes, i.e. egg processing, baking processes, degumming of fats and oils and milk processing for cheese production. Since residual amounts of total organic solids (TOS) are removed in degumming of fats and oils, dietary exposure was calculated only for the remaining three food manufacturing processes. Dietary exposure to the food enzyme-TOS was estimated to be up to 0.41 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 191.2 mg TOS/kg bw per day, the mid-dose tested, which, when compared with the estimated dietary exposure, results in a margin of exposure above 460. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no matches were found. The Panel considered that, under the intended conditions of use, the risk of allergic sensitisation and elicitation reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is considered to be low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Safety evaluation of the food enzyme triacylglycerol lipase from the non-genetically modified Rhizopus arrhizus strain AE-TL(B).

The food enzyme triacylglycerol lipase (triacylglycerol acylhydrolase; EC 3.1.1.3) is produced with the non-genetically modified Rhizopus arrhizus strain AE-TL(B) by Amano Enzyme Inc. The food enzyme was considered free from viable cells of the production organism. It is intended to be used in the modification of fats and oils by interesterification and in the manufacture of enzyme-modified dairy ingredients. Dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.057 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1,960 mg TOS/kg bw per day, the highest dose tested, which, when compared with the estimated dietary exposure, resulted in a margin of exposure of at least 34,386. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions upon dietary exposure cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns, under the intended conditions of use.

Safety evaluation of the food enzyme catalase from porcine liver.

The food enzyme catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.6) is obtained from porcine liver by Avances Bioquímicos Alimentación, S.L. (Spain). The food enzyme is intended to be used in cheese production for decomposition of hydrogen peroxide in brine. The manufacturing process involves the use of a solvent not permitted in the production of foods and food ingredients according to Directive 2009/32/EC. Consequently, the food enzyme does not comply with the existing requirements in the EU.

Safety evaluation of the food enzyme containing trypsin, chymotrypsin, α-amylase and triacylglycerol lipase from porcine pancreas.

The food enzyme complex, containing trypsin (EC 3.4.21.4), chymotrypsin (EC 3.4.21.1), α-amylase (1,4-α-d-glucan glucanohydrolase, EC 3.2.1.1) and triacylglycerol lipase (triacylglycerol acylhydrolase, EC 3.1.1.3), is obtained from porcine pancreas by American Laboratories, Inc., USA. The food enzyme is intended primarily for the hydrolysis of milk proteins to be used in foods for special medical or nutritional dietary management. ■■■■■ is extensively used in the manufacturing process, and residual amounts of the solvent remain in the food enzyme. The applicant estimates a typical range of ■■■■■ in the food enzyme to be 10,000-13,000 mg/kg. Directive 2009/32/EC sets a maximum residue level of 10 mg/kg for foods and food ingredients produced in the EU or imported into the EU. The use of ■■■■■ for the production of a food enzyme falls within the scope of Directive 2009/32/EC. Consequently, the food enzyme does not comply with the existing requirements within the EU governing residual amount of solvent.

Safety evaluation of a food enzyme containing chymosin, pepsin and gastricsin from the abomasum of suckling goats.

The food enzyme containing chymosin (EC 3.4.23.4), pepsin (EC 3.4.23.1) and gastricsin (EC 3.4.23.3) is prepared from the abomasum of suckling goats by Consejo Regulador de la Denominación de Origen Queso Palmero and Consejo Regulador de la Denominación de Origen Queso Majorero. The food enzyme is intended to be used in milk processing for cheese production. As no concerns arise from the animal source of the food enzyme, from its manufacture, and based on the history of safe use and consumption, the Panel considered that toxicological data were not required and no exposure assessment was necessary. Similarity of the amino acid sequences of the three proteins (chymosin, pepsin and gastricsin) to those of known allergens was searched and one match was found. The Panel considered that, under the intended conditions of use, the risk of allergic sensitisation and elicitation reactions by dietary exposure cannot be excluded, but the likelihood is considered to be low. Based on the data provided, the Panel concludes that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Safety evaluation of the native and thermolabile forms of the food enzyme mucorpepsin from Rhizomucor miehei strain MMR 164.

The food enzyme mucorpepsin (aspartic endopeptidase, EC 3.4.23.23) is produced with the non-genetically modified microorganism Rhizomucor miehei strain MMR 164 by Takabio. The enzyme is chemically modified to produce a thermolabile form. The food enzyme is free from viable cells of the production organism. It is intended to be used in milk processing for cheese production. The dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.98 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not raise a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1,320 mg TOS/kg bw per day, the highest dose tested, which when compared with the estimated dietary exposure, resulted in a margin of exposure of at least 1,300. Similarity of the amino acid sequence of the food enzyme to those of known allergens was searched and five matches were found. The Panel considered that, under the intended conditions of use, the risk of allergic sensitisation and elicitation reactions upon dietary exposure to this food enzyme cannot be excluded, but is considered low except for individuals sensitised to mustard proteins, but this risk will not exceed that of mustard consumption. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Safety evaluation of the food enzyme mucorpepsin from Rhizomucor miehei strain DSM 29547.

The food enzyme mucorpepsin (EC 3.4.23.23) is produced with the non-genetically modified Rhizomucor miehei strain DSM 29547 by Chr. Hansen. The food enzyme is free from viable cells of the production organism. It is intended to be used in dairy processing for cheese production. The dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.26 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 618 mg TOS/kg bw per day, the highest dose tested, which when compared with the estimated dietary exposure, results in a margin of exposure of at least 2,400. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and three matches were found. The Panel considered that, under the intended conditions of use, the risk of allergic sensitisation and elicitation reactions by dietary exposure cannot be excluded but is considered low except for individuals sensitised to mustard proteins, but this risk will not exceed that of mustard consumption. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns, under the intended conditions of use.

Safety evaluation of a food enzyme containing aspergillopepsin I and II from the Aspergillus niger var. macrosporus strain PTG8398.

The food enzyme with aspergillopepsin I (EC 3.4.23.18) and aspergillopepsin II (EC 3.4.23.19) activities is produced with a non-genetically modified Aspergillus niger var. macrosporus strain PTG8398 by Meiji Seika Pharma Co., Ltd. The food enzyme was considered free from viable cells of the production organism. It is intended to be used in wine production. Based on the maximum use levels, dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.14 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 919 mg TOS/kg bw per day, the highest dose tested which, when compared with the estimated dietary exposure, results in a margin of exposure above 6,700. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and four matches with respiratory allergens were found. The Panel considered that, under the intended conditions of use, the risk of allergic sensitisation and elicitation reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is considered low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns, under the intended conditions of use.

Safety evaluation of the thermolabile form of the food enzyme mucorpepsin from Rhizomucor miehei strain MMR 164.

The food enzyme mucorpepsin (aspartic endopeptidase, EC 3.4.23.23) is produced with the non-genetically modified microorganism Rhizomucor miehei strain MMR 164. The enzyme is chemically modified by DuPont Nutrition Biosciences (now IFF) to produce a thermolabile form. The food enzyme is free from viable cells of the production organism. It is intended to be used in milk processing for cheese production. The dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.98 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not raise a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1,320 mg TOS/kg bw per day, the highest dose tested, which when compared with the estimated dietary exposure, resulted in a margin of exposure of at least 1,300. Similarity of the amino acid sequence of the food enzyme to those of known allergens was searched and five matches were found. The Panel considered that, under the intended conditions of use, the risk of allergic sensitisation and elicitation reactions upon dietary exposure to this food enzyme cannot be excluded, but is considered low except for individuals sensitised to mustard proteins, but this risk will not exceed that of mustard consumption. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Safety evaluation of the food enzyme mannan endo-1,4-ß-mannosidase from the genetically modified Trichoderma reesei strain RF6232.

The food enzyme mannan endo-1,4-ß-mannosidase (1,4-ß-d-mannan mannanohydrolase; EC 3.2.1.78) is produced with the genetically modified Trichoderma reesei strain RF6232 by AB Enzymes GmbH. The genetic modifications do not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and recombinant DNA. It is intended to be used in coffee processing, fruit and vegetable processing for juice production and for edible oil production. Since residual amounts of total organic solids (TOS) are removed during refined edible oil production by repeated washing, dietary exposure was calculated only for the remaining two food manufacturing processes. Dietary exposure to the food enzyme-TOS was estimated to be up to 0.09 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not raise a safety concern. The systemic toxicity was assessed by a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 100 mg TOS/kg bw per day, the lowest dose tested. This results in a margin of exposure above 1,100. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and one match was found. The Panel considered that, under the intended conditions of use, the risk of allergic sensitisation and elicitation reactions by dietary exposure cannot be excluded, in particular for individuals allergic to avocado, but the likelihood for this to occur is considered to be low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Investigation of thermal changes in the thyroid gland region of individuals with hypothyroidism and fibromyalgia by analyzing the temperature of brown adipose tissue.

This exploratory retrospective study aims to investigate the thermal changes in the thyroid gland region of patients with hypothyroidism and fibromyalgia by analyzing the temperature of the brown adipose tissue (BAT). A total of 166 individuals from 1000 thermographic electronic medical records were classified into four groups: Group HP + FM-50 individuals with hypothyroidism and fibromyalgia; Group FM-56 individuals with fibromyalgia only; Group HP-30 individuals with hypothyroidism only, and Group Control-30 healthy individuals. The thermal images from the electronic medical records were acquired by a FLIR T650SC infrared camera (used for thermometry) and the temperature data for each group were statistically analyzed. Group HP + FM showed r = 0, meaning that the average temperatures of the thyroid and BAT are independent of each other. Groups FM, HP and Control showed r = 1, meaning that the average temperatures of the thyroid and BAT were directly related. Our findings showed that the average temperatures of the thyroid and BAT regions are similar. Also, there was no correlation between thyroid gland temperature and the presence of hypothyroidism or fibromyalgia using thermometry.

Safety evaluation of the food enzyme d-psicose 3-epimerase from the genetically modified Corynebacterium glutamicum strain FIS002.

This assessment addresses a food enzyme preparation consisting of the immobilised intact but non-viable cells of the genetically modified Corynebacterium glutamicum strain FIS002 by CJ-Tereos Sweeteners Europe SAS. The production strain produces the food enzyme d-fructose 3-epimerase (d-psicose 3-epimerase; EC 5.1.3.30). The food enzyme preparation is used in processing fructose to produce a speciality carbohydrate d-allulose (synonym d-psicose). Since residual amounts of total organic solids (TOS) are removed by the purification steps applied during the production of d-allulose, dietary exposure was not calculated. Genotoxicity tests did not raise a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level (NOAEL) of 1,796 mg TOS/kg body weight (bw) per day, the highest dose tested. A search for similarity of the amino acid sequence of the enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic sensitisation and elicitation reactions by dietary exposure cannot be excluded, but the likelihood of such reactions to occur is low. The food enzyme preparation contains multiple copies of an antimicrobial resistance gene, which is considered a hazard. However, under the specific intended conditions of use described by the applicant, and based on the evidence showing the removal of TOS during the production of d-allulose and the absence of recombinant DNA in the d-allulose, the Panel concluded that the identified hazard associated with the food enzyme d-psicose 3-epimerase produced with the genetically modified C. glutamicum strain FIS002 will not result in a risk.