β galactosidase from escherichia coli

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β-galactosidase from Escherichia coli is an enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. It is a widely used tool in molecular biology and biochemistry.

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Escherichia coli (94 citations) β-galactosidase (45 citations) Escherichia coli β-galactosidase (2 citations)

3 protocols using β galactosidase from escherichia coli

Preparation of Tryptophan-Rich Protein Conjugates

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β-galactosidase from Escherichia coli (156 tryptophan residues, PDB 1DP0), β-galactosidase-streptavidin conjugate (180 tryptophan residues), and streptavidin from Streptomyces avidinii (24 tryptophan residues) are purchased from Sigma-Aldrich. The proteins are dissolved in a Hepes buffer (25 mM Hepes, 300 mM NaCl, 0.1 v/v% Tween20, 1 mM DTT, and 1 mM EDTA 1 mM at pH 6.1) which was reported to stabilize β-galactosidase conformation and avoid aggregate formation^{40 (link)}. All the protein stock solutions have been centrifuged for 12 min at 142,000 × g (Airfuge). Just before the optical measurements, GODCAT oxygen scavenger (100 nM glucose oxidase, 830 nM catalase, 10 w/v% D-glucose) with 10 mM DABCO (1,4-Diazabicyclo[2.2.2]octane) is added to the solution to improve the UV photostability^{18 (link)}. p-Terphenyl is also used as received from Sigma-Aldrich and diluted in HPLC-grade cyclohexane.

Barulin A., Roy P., Claude J.B, & Wenger J. (2022). Ultraviolet optical horn antennas for label-free detection of single proteins. Nature Communications, 13, 1842.

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Lipid and Protein Characterization Protocol

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The lipids POPC, 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) were purchased from Avanti Polar Lipids (Alabaster, AL) as powders and used without further purification. Sodium alginate was obtained from Sigma Aldrich (Gillingham, UK) and used without further purification. The MagneHis^TM Ni-Particles were purchased from Promega (Southampton, UK). The secretory phospholipase A2 (sPLA2) from honeybee venom (Apis mellifera), α-Hemolysin from Staphylococcus aureus (α-HL), β-Galactosidase from Escherichia coli and fluorescein di-β-D-galactopyranoside (FDG) were all obtained from Sigma-Aldrich (Gllingham, UK). PDMS Sylgard 184 elastomer kits were purchased from Dow Corning (Michigan, USA). Rhodamine B-labeled alginate was purchased from HAworks (New Jersey, USA). EDDA was purchased from Tokyo chemical industry. The remaining reagents which include sucrose, glucose, Bovine Serum Albumin (BSA), cholesterol, HEPES buffer, potassium chloride, calcium chloride, zinc acetate, ethylenediaminetetraacetic acid (EDTA), sorbitan monooleate (Span 80), mineral oil, sephradex G-50, and 70-kDa-Fluorescein isothiocyanate-dextran were all purchased from Sigma Aldrich (Gillingham, UK) unless specified.

Allen M.E., Hindley J.W., O’Toole N., Cooke H.S., Contini C., Law R.V., Ces O, & Elani Y. (2023). Biomimetic behaviors in hydrogel artificial cells through embedded organelles. Proceedings of the National Academy of Sciences of the United States of America, 120(35), e2307772120.

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Purification and Sample Preparation of GroEL and β-galactosidase

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Chaperonin 60 (GroEL) and β-galactosidase from Escherichia coli were purchased as lyophilized powders from Sigma-Aldrich. Both proteins were dissolved in 100 mM ammonium acetate at ~1 mg/mL. GroEL was precipitated by mixing 200 μL acetone in 100 μL protein solution and allowing the mixture to sit for 5 min. The mixture was centrifuged at 14,000 g for 5 minutes, the liquid was pipetted out, and the precipitate was resuspended in 100 μL of 100 mM NH4OAc. This solution was filtered three times using Amicon Ultra-0.5 centrifugal filters with a molecular weight cut-off of 100 kDa. Each rinse used 400 μL 100 mM NH4OAc. The protein was recovered by inverting the filter and running the centrifuge at 2,000 g for 2 min. β-galactosidase was filtered three times and collected using the same Amicon filters and the same centrifuge settings. Polypropylene glycol (PPG, molecular weight ~2700) was purchased from Sigma-Aldrich. TEM grids (carbon support film on 400 mesh copper) and 1% uranyl acetate staining solution were purchased from Electron Microscopy Sciences.

Lee K.W., Salome A.Z., Westphall M.S., Grant T, & Coon J.J. (2023). Onto grid purification and 3D reconstruction of protein complexes using matrix-landing native mass spectrometry. Journal of proteome research, 22(3), 851-856.

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