Heat capacities of l-histidine, l-phenylalanine, l-proline, l-tryptophan and l-tyrosine

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F21%3A43922435" target="_blank" >RIV/60461373:22340/21:43922435 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22810/21:43922435

Výsledek na webu

<a href="https://doi.org/10.3390/molecules26144298" target="_blank" >https://doi.org/10.3390/molecules26144298</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/molecules26144298" target="_blank" >10.3390/molecules26144298</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Heat capacities of l-histidine, l-phenylalanine, l-proline, l-tryptophan and l-tyrosine

Popis výsledku v původním jazyce

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. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Název v anglickém jazyce

Heat capacities of l-histidine, l-phenylalanine, l-proline, l-tryptophan and l-tyrosine

Popis výsledku anglicky

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. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

<a href="/cs/project/GA19-02889S" target="_blank" >GA19-02889S: Stabilita amorfních pevných disperzí: Predikce pomocí stavových rovnic SAFT a jejich experimentální ověření</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Molecules

ISSN

1420-3049

e-ISSN

—

Svazek periodika

26

Číslo periodika v rámci svazku

14

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

12

Strana od-do

4298

Kód UT WoS článku

000676354700001

EID výsledku v databázi Scopus

2-s2.0-85111077064