Pyris 1 differential scanning calorimeter

Manufactured by PerkinElmer

Sourced in United States

The Pyris 1 Differential Scanning Calorimeter is a laboratory instrument used to measure the thermal properties of materials. It provides quantitative and qualitative information about physical and chemical changes that involve endothermic or exothermic processes, or changes in heat capacity. The instrument can be used to analyze a wide range of materials, including polymers, composites, pharmaceuticals, and foods.

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Lab products found in correlation

Originpro 2019b, by OriginLab (1 mentions) Phi 5000 versaprobe, by Physical Electronics (1 mentions) Zetasizer nano z, by Malvern Panalytical (1 mentions) Originpro 8, by OriginLab (1 mentions)

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Pyris 1 (172 citations) Differential scanning calorimeter (29 citations) Pyris 1 calorimeter (5 citations)

7 protocols using pyris 1 differential scanning calorimeter

Thermostability Analysis of Phytase Variants

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Example 2

To determine the thermostability of the phytases a Perkin-Elmer Pyris 1 Differential Scanning calorimeter (DSC) was employed to determine melting temperatures (T_m) of the phytase variants. The T_manalysis was performed at pH 5.5 (similar to an aqueous feed extract) using 100 mM Citrate as buffer. DSC runs were run with or without 10% Sorbitol-10% NaCl. DSC analysis indicates that 10% Sorbitol-10% NaCl improved the thermostability of the phytascs. In liquid form, T_mgreater than 98° C. can be achieved (FIG. 2). Pseudomonas-expressed phytases showed ˜1-2° C. lower T_mthan the Pichia-expressed phytases in buffer alone, however this temperature reduction was not observed when 10% Sorbitol-10% NaCl was added (FIG. 3).

US10982199B2. Phytase (2021-04-20). BASF Enzymes LLC [US]. Inventors: Xuqiu Tan [US], Arne I. Solbak, Jr. [US].

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Thermostability of Phytase Enzymes

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Example 2

To determine the thermostability of the phytases a Perkin-Elmer Pyris 1 Differential Scanning Calorimeter (DSC) was employed to determine melting temperatures (T_m) of the phytase variants. The T_manalysis was performed at pH 5.5 (similar to an aqueous feed extract) using 100 mM Citrate as buffer. DSC runs were run with or without 10% Sorbitol-10% NaCl. DSC analysis indicates that 10% Sorbitol-10% NaCl improved the thermostability of the phytases. In liquid form, T_mgreater than 98° C. can be achieved (FIG. 2). Pseudomonas-expressed phytases showed ˜1-2° C. lower T_mthan the Pichia-expressed phytases in buffer alone, however this temperature reduction was not observed when 10% Sorbitol-10% NaCl was added (FIG. 3).

US10093909B2. Phytase (2018-10-09). BASF Enzymes LLC [US]. Inventors: Arne I. Solbak, Jr. [US].

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Thermostability of Engineered Phytases

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Example 2

To determine the thermostability of the phytases a Perkin-Elmer Pyris 1 Differential Scanning calorimeter (DSC) was employed to determine melting temperatures (T_m) of the phytase variants. The T_manalysis was performed at pH 5.5 (similar to an aqueous feed extract) using 100 mM Citrate as buffer. DSC runs were run with or without 10% Sorbitol-10% NaCl. DSC analysis indicates that 10% Sorbitol-10% NaCl improved the thermostability of the phytases. In liquid form, T_mgreater than 98° C. can be achieved (FIG. 2). Pseudomonas-expressed phytases showed ˜1-2° C. lower T_mthan the Pichia-expressed phytases in buffer alone, however this temperature reduction was not observed when 10% Sorbitol-10% NaCl was added (FIG. 3).

US09879238B2. Phytase (2018-01-30). BASF Enzymes LLC [US]. Inventors: Xuqiu Tan [US], Arne I. Solbak, Jr. [US].

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Thermostability of Phytase Variants

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Example 2

To determine the thermostability of the phytases a Perkin-Elmer Pyris 1 Differential Scanning calorimeter (DSC) was employed to determine melting temperatures (T_m) of the phytase variants. The T_manalysis was performed at pH 5.5 (similar to an aqueous feed extract) using 100 mM Citrate as buffer. DSC runs were run with or without 10% Sorbitol-10% NaCl. DSC analysis indicates that 10% Sorbitol-10% NaCl improved the thermostability of the phytascs. In liquid form, T_mgreater than 98° C. can be achieved (FIG. 2). Pseudomonas-expressed phytases showed ˜1-2° C. lower T_nithan the Pichia-expressed phytases in buffer alone, however this temperature reduction was not observed when 10% Sorbitol-10% NaCl was added (FIG. 3).

US10550371B2. Phytase (2020-02-04). BASF Enzymes LLC [US]. Inventors: Xuqiu Tan [US], Arne I. Solbak, Jr. [US].

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Thermal Analysis of Biodegradable Polymers

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DSC was performed on the initial samples as well as on the 6, 12, and 24 month follow-up explanted samples. The DSC setup consisted of a PerkinElmer Pyris 1 Differential Scanning Calorimeter (Fremont, CA, USA) and was performed under an inert atmosphere of ultra-high purity N₂. Indium was used for calibration. The 8–11 mg samples were cooled to 0 °C at 300 °C/min, held for 1 min and then heated to 200 °C at 10 °C/min. The glass transition temperature (T_g; onset and midpoint), melting temperature (T_m; onset and midpoint), and melting enthalpy (ΔH_m) were determined using OriginPro 2019b (OriginLab Corporation, Northampton, MA, USA). The degree of crystallinity was calculated using the following formula [55 (link)]: where X_c is the degree of crystallinity (%), ΔH_m the determined melting enthalpy of the copolymer (J/g), ΔH* the melting enthalpy of 100% crystalline PLLA (J/g), and Φ_PLLA the weight fraction of LLA segments in the copolymer. The melting enthalpy of 100% crystalline PLLA is 93 J/g [56 ].

Gareb B., van Bakelen N.B., Driessen L., Buma P., Kuipers J., Grijpma D.W., Vissink A., Bos R.R, & van Minnen B. (2022). Biocompatibility and degradation comparisons of four biodegradable copolymeric osteosynthesis systems used in maxillofacial surgery: A goat model with four years follow-up. Bioactive Materials, 17, 439-456.

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Characterization of UiO-67 Conjugates

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The size of UiO-67 conjugates was measured by JEM-2100 transmission electronic microscopy (TEM, JOEL Ltd., Tokyo, Japan) and the dynamic laser scattering (DLS) measurement was carried out on Zetasizer Nano ZS (Malvern Panalytical, UK). UV–Vis spectra were recorded in a Perkin-Elmer Lambda 390 spectrometer. X-ray photoelectron spectroscopy (XPS) for UiO-67 was conducted on a PHI5000 VersaProbe (ULVAC-PHI, Japan). Thermogravimetric analysis (TGA) was carried out on a Pyris 1 differential scanning calorimeter (Perkin-Elmer).

Cong Y., Sun B., Hu J., Li X., Wang Y., Zhang J., Yang D., Lu W., Ding Z., Wang X, & Hong H. (2022). A carbon monoxide releasing metal organic framework nanoplatform for synergistic treatment of triple-negative breast tumors. Journal of Nanobiotechnology, 20, 494.

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Thermal Analysis of Carp Protein Isolates

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A Perkin-Elmer Pyris-1 differential scanning calorimeter (Waltham, MA, USA) was employed to study the thermal properties of CPIs. Indium was used as standard (melting point 156.6 °C, enthalpy change 28.46 J/g) for temperature and heat flow calibration. Hermetically sealed aluminum pans were prepared to hold 15-20 mg of treated and untreated A8 and A10 suspended in water (15 g/100 g protein).
Samples were scanned at 5 °C/min from 25 to 105 °C. As a reference, an empty pan was used. The denaturation temperatures (T d °C), and the enthalpy change of transition (ΔH J/g dry protein), were obtained by analyzing the thermograms with the OriginPro 8 software (OriginLab Corporation, Northampton, MA, USA).
The degree of protein denaturation (DD) was calculated according to the following equation:
where ΔH o and ΔH t are the enthalpy changes corresponding to the untreated and treated sample, respectively.

Peyrano F., Speroni F, & Avanza M.V. (2016). Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure. Innovative Food Science and Emerging Technologies., 33.

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