Recent advances in phosphorylation of food proteins: A review

Li, Can-Peng; Enomoto, Hirofumi; Hayashi, Yujiro; Zhao, Hui; Aoki, Takayoshi

doi:10.1016/j.lwt.2010.03.016

Cited by 68 publications

(36 citation statements)

References 44 publications

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“…Under alkaline conditions, STMP is hydrolyzed to produce sodium tripolyphosphate, which is believed to phosphorylate serine, threonine, and tyrosine residues through covalent bonding with side-chain oxygen (Gu et al, 2010). That STMP is effective in aiding collagen mineralization, likely via the ability of phosphate groups to attract amorphous calcium phosphate precursors, is supported by prior studies of in vitro mineralization of dentin and dermal collagen (Gu et al, 2010;Li et al, 2010). Meanwhile, the presence of Mg 2+ during mineralization has been shown to improve the stability of PILP and amorphous mineral phases Politi et al, 2009), and allow wetting of protein matrices by PILP (Berg et al, 2013), while incorporation of carbonate during synthetic apatite formation has been shown to result in crystal structures with high similarity to those present in native bone (Chatelain et al, 2013;Liao et al, 2005;Linhart et al, 2001;Moradian-Oldak et al, 1991).…”

Section: Discussionmentioning

confidence: 91%

“…Unlike pAsp and citrate, these were used in the preparation of all mineralized scaffolds produced, and no attempt was made to assess their individual contributions to the mineralized structures produced. STMP has a long history for phosphorylation of proteins in the food industry (Li et al, ; Matheis & Whitaker, ), and phosphorylation of collagen using STMP has previously been described in detail (Gu et al, ; Li & Chang, ; Shen, ). Under alkaline conditions, STMP is hydrolyzed to produce sodium tripolyphosphate, which is believed to phosphorylate serine, threonine, and tyrosine residues through covalent bonding with side‐chain oxygen (Gu et al, ).…”

Section: Discussionmentioning

confidence: 99%

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Use of tendon to produce decellularized sheets of mineralized collagen fibrils for bone tissue repair and regeneration

Grue

Veres

2019

J Biomed Mater Res

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With demand for alternatives to autograft and allograft materials continuing to rise, development of new scaffolds for bone tissue repair and regeneration remains of significant interest. Engineered collagen‐calcium phosphate (CaP) constructs can offer desirable attributes, including absence of foreign body response and possession of inherent osteogenic potential. Despite their promise, current collagen‐CaP constructs are limited to nonload‐bearing applications. In this article, we describe a process for creating decellularized sheets of highly aligned, natively cross‐linked, and mineralized collagen fibrils, which may be useful for developing multilaminate collagen‐CaP constructs with improved mechanical properties. Decellularized bovine tendons were cryosectioned to produce thin sheets of aligned collagen fibrils. Mineralization of the sheets was then performed using an alternate soaking method incorporating a polymer‐induced liquid precursor (PILP) process to promote intrafibrillar mineralization, along with incorporation of physiologically relevant amounts of citrate, Mg, and carbonate. Characteristics of the produced scaffolds were assessed using energy‐dispersive X‐ray spectroscopy (EDX), scanning electron microscopy (SEM), and transmission electron microscopy (TEM). Scaffolds were also compared with both native bovine cortical bone and pure hydroxyapatite using X‐ray powder diffraction (XRD), and Fourier transform infrared spectroscopy attenuated total reflection (FTIR‐ATR). Structural and chemical analyses show that the scaffold preparation process that we described is successful in creating mineralized collagen sheets, possessing a mineral phase similar to that found in bone as well as a close association between collagen fibrils and mineral plates.

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Section: Discussionmentioning

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Use of tendon to produce decellularized sheets of mineralized collagen fibrils for bone tissue repair and regeneration

Grue

Veres

2019

J Biomed Mater Res

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“…Phosphorylation is a covalent modification that adds a phosphate group to a protein or organic molecule. It has emerged as one of the most prominent types of post‐translational modification during evolution and has been shown to improve the functional properties of food proteins . This process occurs in both prokaryotes and eukaryotes, triggering conformational changes in many enzymes and receptors that result in their activation and deactivation.…”

Section: Introductionmentioning

confidence: 99%

Role of phosphate groups on antiviral activity of casein phosphopeptide against feline calicivirus as a surrogate for norovirus

Lebetwa

Mitani

Nakamura

et al. 2016

J. Sci. Food Agric.

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“…In particular the mild reaction conditions and reduced production of waste encouraged the development of enzyme-based technologies. Moreover, in contrast to chemical procedures, enzymes carry out phosphorylations with high regio and stereoselectivity without the need of group protection (Crans & Whitesides, 1985a;Crans & Whitesides, 1985b;Gross, Abril, Lewis, Geresh, & Whitesides, 1983;Li, Enomoto, Hayashi, Zhao, & Aoki, 2010). Kinases are well-known phosphorylating enzymes which transfers a phosphate unit from ATP to a variety of acceptors but the large-scale application is impeded by the need of regenerating ATP and in addition these enzymes are specific for the substrate to be phosphorylated (Faber, 2004).…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation by Alkaline Phosphatase: Immobilization and Synthetic Potential

Babich¹,

Peralta²,

Hartog³

et al. 2013

IJC

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Phosphatases (AP, E.C. 3.1.3.1) are hydrolytic enzymes that naturally hydrolyse phosphomonoesters but in a so-called transphosphorylation reaction these enzymes are also able to transfer a phosphate group from phosphorylated compounds to alcoholic functions. This transphosphorylation catalysed by acid phosphatases using pyrophosphate as a phosphate donor has been studied in some detail. However, the acidic pH optimum of these enzymes limits some of their applications. The catalytic features of alkaline phosphatase are similar to the acid phosphatases and its alkaline pH optimum suggests a possible application of this enzyme in phosphorylation reactions which need to be carried out at higher pH. Here we explore the synthetic potential of bovine intestine alkaline phosphatase (AP) in the phosphorylation of dihydroxyacetone (DHA) and glycerol using pyrophosphate (PP i ) as phosphate donor. The phosphorylated compounds are intermediates in two multi-enzymatic cascade reactions for the synthesis of carbohydrates. The yields of dihydroxyacetone phosphate (DHAP) and glycerol-1-phosphate at pH 8 (2.6 mM and 2.2 mM, respectively) were comparable to the results obtained with the acid phosphatases at pH 4. Nevertheless, when the cascade reactions were carried out at pH 8, very low conversions were measured due to inactivation of the alkaline phosphatase by the product phosphate. To circumvent this inhibition, the alkaline phosphatase was immobilized on aldehyde-activated beads (Sepabeads EC-HA). The immobilization greatly diminished the inhibition by phosphate, and the immobilized alkaline phosphatase at pH 8 gave the same conversions in the cascade reaction starting from DHA as obtained with the acid phosphatase at pH 6. However, the immobilized enzyme was active for only one catalytic cycle and the beads could not be reused.

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Recent advances in phosphorylation of food proteins: A review

Cited by 68 publications

References 44 publications

Use of tendon to produce decellularized sheets of mineralized collagen fibrils for bone tissue repair and regeneration

Use of tendon to produce decellularized sheets of mineralized collagen fibrils for bone tissue repair and regeneration

Role of phosphate groups on antiviral activity of casein phosphopeptide against feline calicivirus as a surrogate for norovirus

Phosphorylation by Alkaline Phosphatase: Immobilization and Synthetic Potential

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