Self-assembly of partially hydrolysed α-lactalbumin

Ipsen, Richard; Otte, Jeanette

doi:10.1016/j.biotechadv.2007.07.006

Cited by 96 publications

(86 citation statements)

References 6 publications

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“…Then Ca 2+ ion has a high affinity for the wellknown (primary) Ca 2+ binding site and stabilizes the native conformation upon binding and a secondary binding site was located 0.8 nm away from the primary binding site [20]. The folding and subsequent assembly of polypeptide chains reaction between the molecules is believed to be the sum of β-sheet stacking involving Hbonds (β-sheet) and Ca 2+ ion bridges between specific carboxylates and amino acids, fixing the molecules in the right orientation in the assembly [21]. Reliance on magic power of self-assembly, actually we just provide specific conditions via chemical hydrolysis and surfactants in make two-dimensional arrays that twist to form hollow cylindrical filaments, with a diameter of about 3 -8 nm single walled nanotubes and finally stacking of ringshaped cyclic peptide subunits leads to protein nanotube formation [6].…”

Section: The Proposed Formation Mechanism Of Protein Nanotubesmentioning

confidence: 99%

Synthesis and Characterization of Various Protein <i>α</i>-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method

Esmaeilzadeh¹,

Fakhroueian²,

Esmaeilzadeh³

et al. 2013

ANP

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New water-based nanofluids including unparalleled milk protein α-lactalbumin hollow nano-bio-tubes using low cost, available and advanced partial chemical hydrolysis strategy in bottom-up nano-assembly have been employed in this work. The aqueous sol-gel chemistry in nanotechnology which we selected for this goal offers new fabrication as interesting smart protein nanotubes. The kinds of nanometer sized tubular structures such as waved, helically coiled, bent, bamboo-shaped, bead-like and branched single-walled protein nanotubes (SWPNTs) with a range of 3 -8 nm in outer diameters were produced by this method. Complete characterization for natural produced nanotubes including SEM, TEM images, G bond and D bond in Raman spectroscopy, XRD patterns, DLS (Dynamic Light Scattering) and FTIR analysis were evaluated which they are most significant experiments in synthesized protein nanotubes soluble in clear water nanofluids and stabilization of transparent nanofluids was proved within more than one year after preparation. Various necessary ligand ion salts such as Mn 2+ , Zn 2+ and Ca 2+ or mixtures as bridge makers and producing biological self-assembly hollow SWPNTs were performed and we focused on new chemical technology under specific acidic hydrolysis method not conventional enzymatic proteolysis and applying surfactants, pH reagent, Tris-HCl buffer, polar solvent which could be produced by β-sheet stacked hydrolysed protein α-lactalbumin mechanism under appropriate conditions to achieving high efficiency new protein nanotubes skeleton. They can be promising materials applied in food science, diet nutrition, nanomedicine, nano-biotechnology and surgery.

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Section: The Proposed Formation Mechanism Of Protein Nanotubesmentioning

confidence: 99%

Synthesis and Characterization of Various Protein <i>α</i>-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method

Esmaeilzadeh¹,

Fakhroueian²,

Esmaeilzadeh³

et al. 2013

ANP

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“…Furthermore, it represents the best characterized model of the intermediate folding structure, the molten globule state, formed upon removal of Ca 2+ by lowering the pH to below 4, or by using chelating agent such as EDTA at neutral pH (Kuwajima 1996). In addition, α-La has been shown to form nanotubular structures upon limited proteolysis (Ipsen et al 2001a), which in turn can result in formation of strong transparent gels and provide the possibility for α-La to be used as a thickening agent or gelling agent in food systems or for encapsulation of bioactive compounds (Ipsen and Otte 2007). However, this nanostructure only forms when α-La occurs in high purity without the presence of β-Lg (Ipsen et al 2001b).…”

Section: Introductionmentioning

confidence: 99%

Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration

Geng

Tolkach

Otte

et al. 2015

Dairy Sci. & Technol.

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A method based on anion exchange chromatography (AIEX) in combination with ultrafiltration (UF) was developed to obtain kilogram-scale amounts of bovine α-lactalbumin (α-La) of high purity from α-La-enriched whey protein concentrate (αWPC). Initially, α-La was successfully purified, at laboratory scale, from a 10% solution of αWPC. Removal of casein and denatured whey protein by acid precipitation resulted in a α-La purity of 78%. A further purification by AIEX eluting with sodium acetate (NaAc) buffer led to a final purity and recovery of 100 and 85%, respectively. Based on this, the process was simplified and optimized for pilot-scale purification by selective binding of β-lactoglobulin (β-Lg). Batchwise expanded bed AIEX using a column with 5 L of Q Sepharose matrix was performed. Pure α-La was obtained in the run through buffer. In the end, 1100 g of holo form α-La was obtained with a purity of 97.4% in protein and a recovery of 80%, calculated based on the protein detectable in reversed phase high-performance liquid chromatography (RP-HPLC). Thus, by combining AIEX and UF, heating was avoided allowing production of α-La in kilo-scale with high purity and recovery from αWPC with a minimum volume of buffer solutions.

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“…The second is planned obsolescence, whereby components of the complex, such as CD14, are degraded before reaching the colon thereby minimizing CD14-dependent inflammation. Alpha-lactalbumin also presents an interesting structural paradigm because of its ability to form nanotubes (35,36), which in the hydrolytic environment of the GI tract may function as a scaffold to shield sCD14 and other bioactive milk components from degradation.…”

Section: Discussionmentioning

confidence: 99%

Alpha-Lactalbumin in Human Milk Alters the Proteolytic Degradation of Soluble CD14 by Forming a Complex

et al. 2010

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ABSTRACT:Mother's milk represents a foundational step in the proper development of newborn immunity. This is achieved, in part, through the action of numerous regulatory proteins such as soluble cluster of differentiation 14 (sCD14) found in significant quantities in human milk (ϳ25-50 g/mL). In adults, CD14 stimulates cytokine production in response to lipopolysaccharide (LPS), the major lipid component found in the outer membrane of Gram-negative bacteria. However, the fate and function of sCD14 in the neonatal gastrointestinal (GI) tract are unknown and may function differently from adults. Therefore, we administered human sCD14 to experimental animals and observed that it persisted in the upper GI tract after feeding. In our search for potential proteolytic protectants, immunoprecipitation of sCD14 from human milk revealed a 15-kD novel protein that copurified with sCD14. Mass spectrometry analysis of the protein identified alpha-lactalbumin. CD14 was also identified by immunoblot after immunoprecipitation of alpha-lactalbumin from milk. In vitro digestion assays revealed that purified alphalactalbumin decreases the proteolytic degradation of human milk derived sCD14 in vitro, suggesting a mechanism by which this key LPS receptor may remain functional in the neonate gut.

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Self-assembly of partially hydrolysed α-lactalbumin

Cited by 96 publications

References 6 publications

Synthesis and Characterization of Various Protein <i>α</i>-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method

Synthesis and Characterization of Various Protein <i>α</i>-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method

Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration

Alpha-Lactalbumin in Human Milk Alters the Proteolytic Degradation of Soluble CD14 by Forming a Complex

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Self-assembly of partially hydrolysed α-lactalbumin

Cited by 96 publications

References 6 publications

Synthesis and Characterization of Various Protein &lt;i&gt;α&lt;/i&gt;-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method

Synthesis and Characterization of Various Protein &lt;i&gt;α&lt;/i&gt;-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method

Pilot-scale purification of α-lactalbumin from enriched whey protein concentrate by anion-exchange chromatography and ultrafiltration

Alpha-Lactalbumin in Human Milk Alters the Proteolytic Degradation of Soluble CD14 by Forming a Complex

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Synthesis and Characterization of Various Protein <i>α</i>-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method

Synthesis and Characterization of Various Protein <i>α</i>-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method