Melting properties of amino acids and their solubility in water

Tam, Hoang; Chua, Yeong Zen; Kumar, Aarti; Pabsch, Daniel; Hallermann, Moritz; Zaitsau, Dzmitry H.; Schick, Christoph; Held, Christoph

doi:10.1039/d0ra08947h

Cited by 60 publications

(52 citation statements)

References 51 publications

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“…); this is reflected by relatively large range of reported decomposition temperatures. Note that the temperatures of fusion reported by Do et al [22] (see Table 2) are higher than those of decomposition by (50 to 140) K. To avoid the decomposition, Do et al [22] used scanning rates up to 20,000 K•s −1 .…”

Section: Thermogravimetric Analysis (Tga)mentioning

confidence: 96%

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Heat Capacities of l-Arginine, l-Aspartic Acid, l-Glutamic Acid, l-Glutamine, and l-Asparagine

et al. 2021

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In an effort to establish reliable thermodynamic data for amino acids, heat capacity and phase behavior is reported for l-arginine (CAS RN: 74-79-3), l-aspartic acid (CAS RN: 56-84-8), l-glutamic acid (CAS RN: 56-86-0), l-glutamine (CAS RN: 56-85-9), and l-asparagine (CAS RN: 70-47-3). Prior to heat capacities measurement, thermogravimetric analysis was performed to determine decomposition temperatures. Crystal heat capacities of all five amino acids were measured by Tian-Calvet calorimetry in the temperature interval (262-358) K and by power compensation DSC in the temperature interval (215-451) K. Experimental values of this work were combined with the literature data obtained with adiabatic calorimetry. Low temperature heat capacities of l-arginine and l-asparagine, for which no or limited literature data were available, were measured using the relaxation (heat pulse) calorimetry. As a result, reference heat capacities and thermodynamic functions for crystalline phase from near 0 K to 450 K were developed. Keywords Crystalline phase • Heat capacity •This article is part of the Special Issue in Memory of Professor Talgat Khasanshin.

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Section: Thermogravimetric Analysis (Tga)mentioning

confidence: 96%

“…a Fast scanning DSC was used by Do et al[22] for T fus determination (see text).b "Temperature of fusion" (in fact T decomp ) recommended by the Syracuse Research Corporation and used by many authors. c Start of the TGA peak (onset not reported).…”

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confidence: 99%

Heat Capacities of l-Arginine, l-Aspartic Acid, l-Glutamic Acid, l-Glutamine, and l-Asparagine

et al. 2021

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“…In the case of l -proline, the first small peak at 484 K does not seem to be accompanied by any mass loss, pointing to a possible crystal–crystal transition. Note that the temperatures of fusion reported by Do et al [ 17 ] (see Table 1 ) are higher than those of decomposition by (20 to 100) K. In order to avoid decomposition, Do et al [ 17 ] used scanning rates up to 20,000 K·s −1 .…”

Section: Resultsmentioning

confidence: 99%

“…Values in this table are rounded to the nearest Kelvin. b Fast scanning DSC was used by Do et al [ 17 ] for T fus determination (see text). c “Temperature of fusion” (in fact T decomp ) recommended by the Syracuse Research Corporation and used by many authors.…”

Section: Resultsmentioning

confidence: 99%

Heat Capacities of l-Histidine, l-Phenylalanine, l-Proline, l-Tryptophan and l-Tyrosine

et al. 2021

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In an effort to establish reliable thermodynamic data for proteinogenic amino acids, heat capacities for l-histidine (CAS RN: 71-00-1), l‑phenylalanine (CAS RN: 63-91-2), l‑proline (CAS RN: 147-85-3), l‑tryptophan (CAS RN: 73-22-3), and l-tyrosine (CAS RN: 60-18-4) were measured over a wide temperature range. Prior to heat capacity measurements, thermogravimetric analysis was performed to determine the decomposition temperatures while X-ray powder diffraction (XRPD) and heat-flux differential scanning calorimetry (DSC) were used to identify the initial crystal structures and their possible transformations. Crystal heat capacities of all five amino acids were measured by Tian–Calvet calorimetry in the temperature interval from 262 to 358 K and by power compensation DSC in the temperature interval from 307 to 437 K. Experimental values determined in this work were then combined with the literature data obtained by adiabatic calorimetry. Low temperature heat capacities of l‑histidine, for which no literature data were available, were determined in this work using the relaxation (heat pulse) calorimetry from 2 K. As a result, isobaric crystal heat capacities and standard thermodynamic functions up to 430 K for all five crystalline amino acids were developed.

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“…Differential Scanning Calorimetry (DSC), due to chemical decomposition (degradation) [16].With the access to high scanning rates with Fast Scanning Calorimetry (FSC), thermodynamic properties such as melting properties can be directly measured, especially for biomolecules without decomposition [17,18]. Recently, an experimental FSC method has been developed for the successful determination of the melting properties of amino acids [19,20], peptides [21,22], nucleobases [23,24], bio-polymers [17,18] and low molecular mass pharmaceuticals [25].…”

Section: Introductionmentioning

confidence: 99%

The melting properties of D-α-glucose, D-β-fructose, D-sucrose, D-α-galactose, and D-α-xylose and their solubility in water: A revision

et al. 2021

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Saccharides are still commonly isolated from biological feedstock by crystallization from aqueous solutions. Precise thermodynamic data on solubility are essential to optimize the downstream crystallization process. Solubility modeling, in turn, requires knowledge of melting properties. In the first part of this work, following our previous work on amino acids and peptides, D-α-glucose, D-β-fructose, D-sucrose, D-α-galactose, and D-α-xylose were investigated with Fast Scanning Calorimetry (FSC) in a wide scanning rate range (2000 K·s−1 to 10000 K·s−1). Using the experimental melting properties of saccharides from FSC allowed successfully modeling aqueous solubility for D-sucrose and D-α-galactose with the equation of state PC-SAFT. This provides cross-validation of the measurement methods to determine accurate experimental melting properties with FSC. Unexpectedly, the experimental FSC melting temperatures, extrapolated to zero scanning rates for thermal lag correction, were higher than results determined with DSC and available literature data. To clarify this inconsistency, FSC measurements towards low scanning rates from 10000 K·s−1 to 1 K·s−1 (D-α-glucose, D-β-fructose, D-sucrose) overlapping with the scanning rates of DSC and literature data were combined. At scanning rates below 1000 K·s−1, the melting properties followed a consistent non-linear trend, observed in both the FSC and the literature data. In order to understand the non-linear decrease of apparent melting temperatures with decreasing heating rate, the endothermic peaks were investigated in terms of isoconversional kinetics. The activation energies in the non-linear dependency region are in the range of $$300<{E}_{A}< 600 {\text{kJ}}\bullet {\text{mo}}{\text{l}}^{-1}$$ 300 < E A < 600 kJ ∙ mol - 1 . These values are higher than the enthalpy of sublimation for D-α-glucose, indicating that the non-linear behavior does not have a physical nature but attributes to chemical processes corresponding to the decomposition of molecular compounds within the crystal lattice before melting. The melting properties reported in the literature, commonly determined with conventional methods such as DSC, lead to inaccurate results due to the decomposition of these biomolecules at low heating rates. In addition, the FSC results at lower scanning rates coincide with results from DSC and literature in the overlapping scanning rate range, further validating the accuracy of FSC measurements to determine reliable melting properties of thermally labile biomolecules. The experimental FSC melting properties determined at higher scanning rates are considered as the correct equilibrium melting properties, which are not influenced by any chemical processes. The combination of FSC and PC-SAFT opens the door to model solubility of solid compounds that commonly decompose before melting.

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Melting properties of amino acids and their solubility in water

Abstract: We report the melting properties of amino acids for the first time and highlight the usefulness of such data to predict material properties such as aqueous solubility of amino acids.

Cited by 60 publications

References 51 publications

Heat Capacities of l-Arginine, l-Aspartic Acid, l-Glutamic Acid, l-Glutamine, and l-Asparagine

Heat Capacities of l-Arginine, l-Aspartic Acid, l-Glutamic Acid, l-Glutamine, and l-Asparagine

Heat Capacities of l-Histidine, l-Phenylalanine, l-Proline, l-Tryptophan and l-Tyrosine

The melting properties of D-α-glucose, D-β-fructose, D-sucrose, D-α-galactose, and D-α-xylose and their solubility in water: A revision

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