The sample (20 mg) was placed into a hydrolysis tube, followed by the addition of 10 mL 6.0 moL/L hydrochloric acid and 3 drops of phenol. Nitrogen gas was then purged into the tube for 2 min, and the tube was sealed. The hydrolysis tube was placed in a 110 ± 1 °C oven and left for 22 h. After cooling, the hydrolysate was filtered and diluted to 100 mL. The obtained solution (1 mL) was transferred to a 50 mL centrifuge tube and dried in a concentrator at 45 °C. After drying, 1 mL of distilled water was added to dissolve the residue, followed by filtration through a 0.22 µm filter membrane. The amino acid composition, excluding tryptophan, was measured using a Sykam S433D amino acid analyzer (Munich, Germany).
S433d amino acid analyzer
Manufactured by Sykam
Sourced in Germany
The S433D amino acid analyzer is a laboratory instrument designed for the analysis and quantification of amino acids. It utilizes chromatographic techniques to separate and detect individual amino acid components within a sample. The core function of the S433D is to provide accurate and reliable data on the amino acid composition of various biological samples.
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Lab products found in correlation
10 protocols using s433d amino acid analyzer
1
Amino Acid Composition Analysis
2
Characterization of Vinegar Fermentation
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The temperature during the Fermentation was monitored using a thermometer. A total of 10 g of the vinegar pei was added into 30 ml distilled water, agitated at 100 rpm for 3 h at room temperature (20°C), centrifuged for 10 min at 6000 g, and the supernatant collected for the following analysis. The total acid, pH, amino nitrogen, and reducing sugar contents were determined following the previous methods (Huang et al., 2022 (link)). The contents of nine organic acids were analyzed by an Agilent 1,260 high-performance liquid chromatography (HPLC) system (Agilent Corp., Karlsruhe, Germany) with Aminex HPX-87H ion exclusion column (7.8 × 300 mm, i.d., 5 μM) according to the previous research (Wu et al., 2017 (link)). The amino acid content was measured using a Sykam S-433D amino acid analyzer (Sykam GmbH, Bavaria, Germany) (Yang et al., 2021 (link)). The reducing sugar content was measured by the 3,5-dinitrosalicylic acid (DNS) method (Yang et al., 2018 (link)). The contents of volatile compounds were detected by headspace-solid phase microextraction (HS-SPME)/gas chromatography–mass spectrometry (GC–MS) using an Agilent 7890B-5977B GC–MSD system equipped with a DB-wax capillary column (30.0 m × 0.25 mm × 0.25 μm, Agilent Technology, Santa Clara, CA, United States; Jia et al., 2020 (link)). All measurements were carried out in triplicates.
3
Amino Acid Profiling of Rice Flour
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The hydrolyzed amino acids were analyzed by a Sykam S433D amino acid analyzer (Sykam, Munich, Germany) with a column packed with LCA K07/Li. For each treatment group, the brown rice flour from three replicates was mixed and set as the mixed samples. The extraction and analysis were completed according to Weiss et al. [47 (link)]. After acid hydrolysis (6 M hydrochloric acid), quantitation was carried out using an external standard (17 amino acid standards, Yuanye, Shanghai, China) method.
4
Camellia Seed Meal Bioactive Compounds
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Camellia seed meal was obtained from Da Tuan Jie Edible Oil Co., Ltd. (Anhui, China). The alkaline protease (200,000 U/ g) and flavourzyme (23200 U/g) were purchased from Novozymes (Beijing, China). The anhydrous glucose, xylose, ribose, and fructose were procured from Shanghai McLean Biochemical Technology Co., Ltd. DPPH and ABTS reagents were procured from Shanghai Haoyang Biotechnology Co., Ltd. The instruments used were SCION SQ from Brock (Karlsruhe, Germany) and SYKAM S-433D amino acid analyzer (Beijing, China). The infrared analysis was performed using a Therme Fisher Company, Nicolet 6700 (Waltham, MA, USA).
5
Amino Acid Analysis of Bacterial Extracts
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The amino-acid analysis of bacterial cell extracts was conducted on an S-433D amino-acid analyzer (Sykam GmbH, Germany) as described previously [17 ]: Detection was carried out at two wavelengths (570 and 440 nm) according to the manufacturer’s instructions. The separation was performed on a strong acid cation exchange resin with a sulfonic group (PEEK, 4.6 × 150 mm, 7 um). The amino acids were eluted sequentially through the eluent at the rate of 0.45 mL/min at different pH.
6
Beef Extract Preparation and Analysis
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BD was prepared by the previously reported method (18 ). Exactly 1 kg of beef ham was cut into 2-cm3 cubes and minced using a meat grinder. The minced beef was boiled in water (minced beef/water ratio, 1:2) in a pot for regulated by a power regulator for a total of 12 h. Subsequently, oil was skimmed off the resulting BD, the suspension was strained through a colander and further filtered with gauze. BD was concentrated using a rotary evaporator (YaRong Biochemistry Instrument Factory, Shanghai, China) and the final concentrated BD had a volume of 60 ml. It contained 36.34 mg/kg carnosine, which was detected by an S-433D amino acid analyzer (Sykam, Eresing, Germany).
7
Plasma Biochemical Markers Analysis
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Concentrations of plasma amino acids were determined using an S-433D Amino Acid Analyzer (Sykam, Munich, Germany), as described previously (Zhou et al., 2022a (link)). Concentrations of plasma total cholesterol (TC), triglyceride (TG), total protein (TP), endotoxin, and urea nitrogen (UN) were determined using a biochemical analyzer (Bayer, Manufactured Bayer Diagnostics Manufacturing) with commercial kits (Nanjing Jiancheng Bioengineering Institute, Nanjing, China). The activity of plasma glutamic-pyruvic transaminase (GPT), glutamic-oxalacetic transaminase (GOT), alkaline phosphatase (ALP), and lipase was determined using a CX-4 automatic biochemical analyzer (Beckman Institute, California, USA).
8
Amino Acid Profiling of Tea Samples
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Amino acid extracts were prepared as in Section 2.5. An S—433D amino acid analyzer (SYKAM, Munich, Germany), coupled to an LCA K07/Li column (SYKAM, Munich, Germany), was used to detect the amino acids in each tea sample. The elution and derivation flow rates were 0.45 and 0.25 mL/min, respectively. The mobile phases were purchased from SYKAM, including buffer A (0.12 N, pH 2.9), B (0.3 N, pH 4.2), and C (0.3 N, pH 8.0). Buffer D (500 mM NaOH, 0.68 mM EDTA) was prepared inhouse. The detection wavelengths were 440 nm for proline and 570 nm for all other amino acids. The gradient method used for elution was the same as described previously (Yang et al., 2022 (link)). The sixteen amino acids were identified and quantified according to authentic standards and by comparing peak areas for the analytical standards and tea samples; each sample was analyzed in triplicate
9
Amino Acid Composition Analysis
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Amino acid contents weremeasured after acid hydrolysis in accordance with Xu et al. (2015) (link) with some modifications. Hydrolysis of sample was conducted with 6 mol/L HCl at 110 °C for 24 h in a drying oven, and transferred into a 50 ml volumetric flask and diluted to the reticule with distilled water. Then, 1 mL of the filtrate was evaporated at 40–50 °C by rotary evaporator, dissolved in 1–2 mL of distilled water and dried. After complete drying, the residue was diluted with 1 mL of buffer (pH 2.2) and applied to a S433D amino acid analyzer (SYKAM, Eresing, Germany). The amino acids were identified and quantified from standard curves constructed with a mixture standard of threonine (Thr), methionine (Met), valine (Val), isoleucine (Ile), leucine (Leu), phenylalanine (Phe), lysine (Lys), tyrosine (Tyr), histidine (His), arginine (Arg), aspartic acid (Asp), serine (Ser), glutamic acid (Glu), glycine (Gly), alanine (Ala) and proline (Pro) (Sigma Aldrich, St Louis, MO, USA). Because acid hydrolysis oxidises and breaks down tryptophan, these results were not reported.
10
Comprehensive Nutrient Analysis of Herb Residues
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For analysis of nutrient ingredients in target herb residues, the contents of crude protein, crude fiber, crude fat and amino acids were tested by kieldahl apparatus B316 (Buchi, Fluwil, Switzerland), Scino FT350 fiber analyzer (Foss, Hilleroed, Denmark), Soxtec 2043 extraction system (Foss) and S433D amino acid analyzer (Sykam, Munich, Germany), respectively. For purification of compounds, column chromatography (CC) was carried out on silica gel (100–200 mesh and 300–400 mesh, domestic) or Sephadex LH-20 (GE, MA, USA), then semi-preparative reversed phase HPLC was performed on the Waters 1525 HPLC system equipped with a UV/Visible Detector and a Welch Ultimate AQ-C18 column (5 μm, 250 × 10 mm, Welch Materials Inc., Shanghai, China). For structural characterization of compounds, UV spectra, High-resolution mass spectra and NMR spectra were obtained on UV-1700 spectrometer (Shimadzu, Kyoto, Japan), LTQ Orbitrap ETD LC–MS system (Thermo Scientific, MA, USA) and 400 or 500 MHz NMR spectrometer (Brucker, Ettlingen, Germany), respectively. All experiments were performed in triplicate, and the data were expressed as an average value with standard deviation. Differences were considered statistically significant if p < 0.05.
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