Protein-based samples were obtained following a two-stage process: Initially, PPP and glycerol blends were obtained at three different ratios (50/50, 75/25, and 100/0) by using a two-blade counter-rotating Haake Polylab QC batch mixer (ThermoHaake, Karlsruhe, Germany). Blends were obtained at room temperature and 50 rpm for 5 min; subsequently, protein-based samples were obtained after the processing of blends by the Minijet Piston Injection Molding System (ThermoHaake, Karlsruhe, Germany). Cylindrical specimens (10 mm diameter, 15 mm length) were obtained at 60 • C and 500 bar pressure for 150 s [17] . Superabsorbent matrices were generated after submitting protein-based samples to 48 h of water immersion and subsequent drying either in a conventional oven or by freezedrying. On the one hand, the samples were placed in a UN55 oven (Memmert, Germany) at 50 • C for 24 h. Samples were subjected to heat-drying under natural convection conditions (in the absence of any forced air circulation). On the other hand, the samples were first conveniently frozen at -40 • C for 24 h in a static freezer (Model EVF 110/45; Equitec, Madrid, Spain), and then they were freeze-dried in vacuum flasks fitted to an 8-port manifold of a LyoQuest freeze-dryer (Telstar Technologies, Barcelona, Spain) (condenser temperature: -85 • C; temperature of sample holder: room temperature; pressure: 0.01 mbar).
Lyoquest freeze dryer
Manufactured by Telstar
Sourced in Spain
The LyoQuest freeze-dryer is a laboratory equipment designed for the process of lyophilization, also known as freeze-drying. It is used to remove water from samples through a combination of freezing and vacuum drying, preserving the structure and properties of the material. The core function of the LyoQuest is to facilitate this freeze-drying process in a controlled environment.
Automatically generated - may contain errors
Lab products found in correlation
Frontier ft ir spectrometer, by PerkinElmer (2 mentions)
Flask m8 head, by Telstar (2 mentions)
Un55 oven, by Memmert (1 mentions)
Su 70, by Hitachi (1 mentions)
Tribute peptide synthesizer, by Protein Technologies (1 mentions)
Zorbax c18 column, by Agilent Technologies (1 mentions)
Agilent zorbax c18 column, by Agilent Technologies (1 mentions)
Acclaim 120 c18 column, by Thermo Fisher Scientific (1 mentions)
Microtof q 2, by Bruker (1 mentions)
Ultra turrax homogenizer, by IKA Group (1 mentions)
Celluclast, by Novozymes (1 mentions)
Spectrum 10, by PerkinElmer (1 mentions)
Geminisem 500, by Zeiss (1 mentions)
20 protocols using lyoquest freeze dryer
1
Protein-Based Superabsorbent Matrix Fabrication
2
Freeze Drying Nanostructured Lipid Carriers
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The NLC formulations were frozen for 12 h at −80 °C and lyophilized at a pressure of 0.1 mbar for 24 h at −40 °C using a Telstar LyoQuest Freeze Dryer (Barcelona, Spain). The production yield (YNLC) was calculated by Equation (2).
3
Persimmon Fruit Characterization Protocol
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For analysis, six batches, a total of 192 units (32 per batch) of persimmon fruits, were received from November to December 2017 (batches K1, K2 and K3) as well as in November 2018 (batches K4, K5 and K6). Approximately 8–11 units from each batch were randomly selected and weighed, and the values were recorded in order to calculate the mean weight. On the same day, fruits were fully peeled leaving the edible pulp of the fruit.
Half of each fruit was homogenized for analysis required on fresh fruits. The other half was sliced and frozen at −20 °C for a minimum of 24 h in order to prepare the dry sample useful for further analysis. Subsequently, a Telstar LyoQuest freeze-dryer was employed for freeze-drying and preservation of the samples. The fruits were kept in the freeze-dryer protected from light, to ensure its conservation, at −50 °C and a pressure of 0.100 mBar for a minimum of 72 h. The dried persimmon fruits were then homogenized with a domestic Vorwerk Thermomix 3300 mixer. The powdered lyophilized samples were stored in airtight containers, in the dark and at a controlled temperature to avoid alteration of the product. This dried sample was destined for the determination of dietary fiber content, mineral composition and carotenoid content.
Half of each fruit was homogenized for analysis required on fresh fruits. The other half was sliced and frozen at −20 °C for a minimum of 24 h in order to prepare the dry sample useful for further analysis. Subsequently, a Telstar LyoQuest freeze-dryer was employed for freeze-drying and preservation of the samples. The fruits were kept in the freeze-dryer protected from light, to ensure its conservation, at −50 °C and a pressure of 0.100 mBar for a minimum of 72 h. The dried persimmon fruits were then homogenized with a domestic Vorwerk Thermomix 3300 mixer. The powdered lyophilized samples were stored in airtight containers, in the dark and at a controlled temperature to avoid alteration of the product. This dried sample was destined for the determination of dietary fiber content, mineral composition and carotenoid content.
4
SEM Imaging of Listeria monocytogenes Treated with Antimicrobial Agents
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SEM images of bacteria after treatment with Trn αβ loaded liposomes and dissolved thuricin CD peptides were obtained according to a previously developed method (Ratrey et al., 2020 (link)). Briefly, an overnight L. monocytogenes culture was diluted to an OD595 reading of 0.2 and incubated for 24 h at 37 °C with Trn αβ loaded liposome suspension or dissolved thuricin (thuricin powder in 70 % IPA 0.1 % TFA in water and further diluted in PBS) at a concentration of double the observed MIC50. Controls were set with blank liposome suspension and PBS. After incubation, the samples were centrifuged at 300 rcf for 7 min. The supernatant was removed, and the pellet was fixed with 2.5 % glutaraldehyde in PBS overnight at 37 °C. Glutaraldehyde was removed, and the pellet was washed once with PBS and three times with sterile water. This was then freeze-dried in a Telstar Lyoquest freeze dryer at – 80 °C and 0 mbar. The dried cells were placed on a sticky carbon disc onto a metal stub and coated with gold for 120 s at 20 mA in an Emitech K55 system. Images of these L. monocytogenes cells treated with Trn αβ liposomes and dissolved thuricin CD were obtained by SEM on a Hitachi SU-70.
5
Functionalization of Nanostructured Lipid Carriers
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To confirm the functionalization of the NLC with Lf and infer about possible drug–lipid interactions, Fourier transform infrared spectroscopy (FTIR) was performed. The functionalized NLC were previously frozen overnight at −85 °C and lyophilized at −75 °C and 0.4 mBar using a LyoQuest freeze dryer (Telstar, Terrassa, Spain).
The infrared spectra were obtained by placing the samples (riluzole, Precirol® ATO5, molten mixture of the lipids and drug—drug–lipid melt, and functionalized NLC) on a PerkinElmer Frontier™ FTIR Spectrometer (Waltham, MA, USA) equipped with a universal attenuated total reflectance (ATR) attachment and a diamond crystal. For each measurement, 32 scans at a resolution of 4 cm−1 were accumulated at frequencies between 4000 to 600 cm−1.
The infrared spectra were obtained by placing the samples (riluzole, Precirol® ATO5, molten mixture of the lipids and drug—drug–lipid melt, and functionalized NLC) on a PerkinElmer Frontier™ FTIR Spectrometer (Waltham, MA, USA) equipped with a universal attenuated total reflectance (ATR) attachment and a diamond crystal. For each measurement, 32 scans at a resolution of 4 cm−1 were accumulated at frequencies between 4000 to 600 cm−1.
6
Analytical RP-HPLC and ESI-MS for Peptide Synthesis
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Reaction vessels for manual peptide synthesis as well as the automated Tribute peptide synthesizer were from Protein Technologies Inc. Analytical RP-HPLC analysis was performed on an Agilent 1260 series instrument using an analytical Agilent Zorbax C18 column (column dimensions: 150 mm × 4.6 mm, 5 μm particle size) at a flow rate of 1 ml/min. All RP-HPLC analyses were done with 0.1% (v/v) TFA in H2O (RP-HPLC solvent A) and 90% ACN and 0.1% (v/v) TFA in H2O (RP-HPLC solvent B) as mobile phases. Typically, a gradient from 0% to 70% solvent A to solvent B over 30 min was used for analytical RP-HPLC analyses unless otherwise stated. Purification of proteins on a semi-preparative scale were performed on an Agilent 1260 series instrument using a semi-preparative Agilent Zorbax C18 column (column dimensions: 250 mm × 9.4 mm, 5 μm particle size) at a flow rate of 4 ml/min. Lyophilization was carried out with a Telstar LyoQuest freeze dryer. Electrospray ionization mass spectrometric (ESI-MS) analysis was conducted on a Shimadzu MS2020 single quadrupole instrument connected to a Nexera UHPLC system. Mass spectra were acquired by electrospray ionization in positive ion mode in the mass range of 200–2000 m/z.
7
Freeze-drying and UHPLC-HRMS Analysis
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The supernatant (culture media or saline) was concentrated by removing the water using a Lyoquest freeze dryer (Telstar®) at a temperature of −77 °C and vacuum of 0.046 m-bar. Thereafter, samples were diluted in a mixture of water and acetonitrile (1:1). At least 20 μl of each of the samples was injected into an ultimate 3000 ultra-high performance liquid chromatography (U-HPLC) (Thermo Scientific and Dionex) fitted with an Acclaim™ 120 C18 column (Dionex) with a particle size of 3 μm, 2.1 mm × 100 mm diameter and average pore diameter of 120 Å. The mobile phase (0.1% formic acid and water, 0.1% formic acid and acetonitrile) containing formic acid as an ion pairing agent was added to the column at a flow-rate of 0.3 ml/min. The U-HPLC was connected to a MicroTOF-QII (Bruker™) high resolution mass spectrophotometer (MS). Peaks were identified by use of an attached library.
8
Profiling Clementine Fruit Varieties
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Clementine fruits from three extra early varieties of Citrus clementina Hort ex Tan. (Basol, Clemensoon and Clemenrubí) were gathered in their optimal ripening stage in October from a cultivar area near to Valencia (Spain) on three consecutive seasons (2011–2013). In order to obtain a representative sample, amounts of 2 kg (around 23–30 pieces) of each species were randomly selected in optimal conditions for consumption from different trees. After collection, fruits were packed and sent to the lab (UCM in Madrid, Spain) within the same day. All the samples showed a similar external appearance; the thin peel (epicarp) was removed, pulp (mesocarp) was separated and cut into small pieces, and whole fresh pulp was homogenized with an Ultra-Turrax® homogenizer (IKA® Works, Inc., Wilmington, NC, USA). Aliquots of homogenized fresh pulp were taken to perform physico-chemical analysis, and organic acids and vitamin C determination. One portion was immediately freeze-dried (Telstar LyoQuest freeze-dryer, Madrid, Spain) and preserved in hermetic containers at −20 °C, in a dark and dry ambient until used for the analysis of proximate composition, soluble sugars, dietary fiber, mineral composition, individual polyphenols, tocopherols, fatty acids, and antioxidant activity [15 ].
9
Freeze-Dried Apple By-Product Enzymatic Hydrolysis
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Apple by-product obtained from Golden Delicious variety was provided by Zucasa (Zumos Catalano Aragoneses S.A., Huesca, Spain). Once in the laboratory, it was freeze-dried (LyoQuest Freeze Dryer, Telstar S.A. Madrid, Spain), ground into fine powder (particle size <1 mm) and stored in a dry atmosphere. Previously to all analyses, apple by-product was hydrated in distilled water at room temperature with constant shaking Heidolph Reax 2 (speed from 1–9) overnight to simulate raw fresh material conditions.
Enzymatic treatment was performed with Celluclast®, a commercial food-grade cellulase (endo-β-glucanase) from Trichoderma reesei (Novozymes, Bagsvaerd, Denmark).
Enzymatic treatment was performed with Celluclast®, a commercial food-grade cellulase (endo-β-glucanase) from Trichoderma reesei (Novozymes, Bagsvaerd, Denmark).
10
Preparation of Fermented Flours from Whole Grains
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Whole cowpea, whole sorghum, and OFSP were sourced from the Agricultural Research Council, Nelspruit, Fish on Tackle Store, Kempton Park, and Woolworths store, Johannesburg, respectively, all in South Africa. The required chemicals and reagents (analytical grades) were procured from Merck (Darmstadt, Germany) and other notable manufacturers. The WGB and OFSP were dry-cleaned to remove foreign materials. The grains were divided into two batches, where batch A was subjected to the germination process, and batch B was milled in Philips Mill HR2056/90 (Koninklijke Philips N.V., Eindhoven, Netherlands) to prepare fermented flours. The OFSP was thinly peeled, rinsed with water, diced into cubes, lyophilised (Telstar LyoQuest freeze dryer, Terrassa, Spain) and then milled to obtain flour for fermentation. The flours were packed in ziplock bags and stored at 4 °C before further processing.
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