Enzymatic production of biosilica glass using enzymes from sponges: basic aspects and application in nanobiotechnology (material sciences and medicine)

Schröder, Heinz C.; Brandt, David; Schloßmacher, Ute; Wang, Xiaohong; Tahir, Muhammad Nawaz; Tremel, Wolfgang; Беликов, С. И.; Müller, Wernér E.G.

doi:10.1007/s00114-006-0192-0

Cited by 79 publications

(52 citation statements)

References 141 publications

(154 reference statements)

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“…The next tasks for our studies with Monorhaphis will be (i) cloning of the gene encoding silicatein and analysis of the role of the recombinant protein during bio-silica formation and (ii) study of the additional fibrillar structures within and on the spicules. Besides being of general cell biological interest, the information on the silicatein-based formation of glass fibres is of prime biotechnological importance for the application of sponge spicules in (nano)optics (Wang and Wang, 2006;Schröder et al, 2007a;Schröder et al, 2007b).…”

Section: Discussionmentioning

confidence: 99%

Identification of a silicatein(-related) protease in the giant spicules of the deep-sea hexactinellidMonorhaphis chuni

Müller

Boreiko

Schloßmacher

et al. 2008

Journal of Experimental Biology

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SUMMARYSilicateins, members of the cathepsin L family, are enzymes that have been shown to be involved in the biosynthesis/condensation of biosilica in spicules from Demospongiae (phylum Porifera), e.g. Tethya aurantium and Suberites domuncula. The class Hexactinellida also forms spicules from this inorganic material. This class of sponges includes species that form the largest biogenic silica structures on earth. The giant basal spicules from the hexactinellids Monorhaphis chuni and Monorhaphis intermedia can reach lengths of up to 3·m and diameters of 10·mm. The giant spicules as well as the tauactines consist of a biosilica shell that surrounds the axial canal, which harbours the axial filament, in regular concentric, lamellar layers, suggesting an appositional growth of the spicules. The lamellae contain 27·kDa proteins, which undergo post-translational modification (phosphorylation), while total spicule extracts contain additional 70·kDa proteins. The 27·kDa proteins cross-reacted with anti-silicatein antibodies. The extracts of spicules from the hexactinellid Monorhaphis displayed proteolytic activity like the silicateins from the demosponge S. domuncula. Since the proteolytic activity in spicule extracts from both classes of sponge could be sensitively inhibited by E-64 (a specific cysteine proteinase inhibitor), we used a labelled E-64 sample as a probe to identify the protein that bound to this inhibitor on a blot. The experiments revealed that the labelled E-64 selectively recognized the 27·kDa protein. Our data strongly suggest that silicatein(-related) molecules are also present in Hexactinellida. These new results are considered to also be of impact for applied biotechnological studies.

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Section: Discussionmentioning

confidence: 99%

Identification of a silicatein(-related) protease in the giant spicules of the deep-sea hexactinellidMonorhaphis chuni

Müller

Boreiko

Schloßmacher

et al. 2008

Journal of Experimental Biology

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“…It was notable that the enzymes were able to process large nonpolar organosiloxanes, albeit at a low rate. There is currently no experimentally derived structure for any of the silicateins, but previous models (27) 3. Graphs of the extent of hydrolysis of the 4-nitrophenoxy silyl ether substrates 1 (A), 2 (B), and 3 (C) against time, as measured by UV-Vis absorbance at 405 nm corresponding to the 4-nitrophenoxylate anion (calibrated using data from SI Appendix, Fig.…”

Section: Kinetic Analysis Of Tf-silα and Silα-catalyzed Silyl Ether Hmentioning

confidence: 99%

Recombinant silicateins as model biocatalysts in organosiloxane chemistry

Dakhili

Caslin

Faponle

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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The family of silicatein enzymes from marine sponges (phylum Porifera) is unique in nature for catalyzing the formation of inorganic silica structures, which the organisms incorporate into their skeleton. However, the synthesis of organosiloxanes catalyzed by these enzymes has thus far remained largely unexplored. To investigate the reactivity of these enzymes in relation to this important class of compounds, their catalysis of Si-O bond hydrolysis and condensation was investigated with a range of model organosilanols and silyl ethers. The enzymes' kinetic parameters were obtained by a high-throughput colorimetric assay based on the hydrolysis of 4-nitrophenyl silyl ethers. These assays showed unambiguous catalysis with k cat /K m values on the order of 2-50 min. Condensation reactions were also demonstrated by the generation of silyl ethers from their corresponding silanols and alcohols. Notably, when presented with a substrate bearing both aliphatic and aromatic hydroxy groups the enzyme preferentially silylates the latter group, in clear contrast to nonenzymatic silylations. Furthermore, the silicateins are able to catalyze transetherifications, where the silyl group from one silyl ether may be transferred to a recipient alcohol. Despite close sequence homology to the protease cathepsin L, the silicateins seem to exhibit no significant protease or esterase activity when tested against analogous substrates. Overall, these results suggest the silicateins are promising candidates for future elaboration into efficient and selective biocatalysts for organosiloxane chemistry.silicatein | biocatalysis | organosilicon | organosiloxane | silyl ether T he organosiloxanes, compounds containing C-Si-O moieties, represent a class of compounds with a truly diverse range of applications. They are commonly used in the form of polysiloxane "silicone" polymers as components of industrial and consumer products for a variety of purposes such as bulking agents, separation media, protective coatings, lubricants, emulsifiers, and adhesives (1-3). Their use as auxiliaries in the chemical synthesis of complex molecules is also long-established (4-6). However, the production and synthetic manipulation of these compounds are almost entirely dependent on chlorosilane feedstocks, which are environmentally undesirable and energyintensive to produce (7,8). Furthermore, organosiloxanes, which are entirely anthropogenic in origin, are now known to be persistent environmental contaminants because little attempt is made to recover and recycle them (3). Synthetic routes that use, and ultimately recycle, siloxanes and silanols as alternatives would in principle be more environmentally sound.One possible strategy toward improved sustainability is to harness enzymes for chemical processing. Such biocatalysts are attractive because they offer highly efficient synthesis in terms of yields and regio-and stereospecificity, together with an ability to promote reactions under mild conditions and a minimal reliance on halogenated or metallic feedstocks (...

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“…Otherwise, silicatein, silaffin and polyamines have been identified as constituents of the axial filaments in sponges and the cell walls in diatoms. 3,8,9 Although this fact strongly suggests that they process silica in the heterogeneous phase, as far as we know, there is no information about in vitro processes carried out under this conditioning (i.e. on the role of solid phase additives).…”

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confidence: 99%

Biomimetic chitosan-mediated synthesis in heterogeneous phase of bulk and mesoporous silica nanoparticles

et al. 2009

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Both bulk and mesoporous silica nanoparticles can be obtained in the form of granular aggregates using chitosan flakes as additive under very soft biomimetic reaction conditions.Biomineralization, that is the formation under extremely soft conditions of complex hierarchical inorganic materials by biological systems, is an exciting research field of increasing interest. 1 Indeed, while technological silica production usually requires vigorous conditions at high pH, 2 certain marine organisms and some higher plants are capable of forming silica skeletons under mild temperature and pressure conditions at circumneutral pH. 1,3,4 Such in vivo processes generating intricate silica nano and macro-scale patterns are speciesspecific, presumably encoded in the genome; 5-7 the possibility of controlling them in the laboratory remains a long-term major challenge. Notwithstanding, there have been different biomolecules identified like silicatein, silaffin and polyamines, which can play key roles in the hydrolysis, condensation and aggregation of the silica species. 3,4,8 Silica is widely used in industry, medicine and nanotechnology in a huge variety of forms. 2,7,9 This, coupled with the insufficiency of natural products of adequate purity and the scientific interest, justifies the search for bioinspired synthesis 8,10 leading to new silica-based materials with simple hierarchical structures or, at least, allowing silica production under soft-conditions (low-cost strategies). Then, inspired by nature, a variety of reagents have been added to check in vitro silicification processes in solution. 11,12 These additives, which intend to mimic the active natural molecules, can play different roles: catalysts, aggregation promoting reagents or structural directing agents. Otherwise, silicatein, silaffin and polyamines have been identified as constituents of the axial filaments in sponges and the cell walls in diatoms. 3,8,9 Although this fact strongly suggests that they process silica in the heterogeneous phase, as far as we know, there is no information about in vitro processes carried out under this conditioning (i.e. on the role of solid phase additives).Here we show how using solid flakes of chitosan (a commercial and low-cost biopolymer present in the shells of crustaceans and the cell walls of fungi and yeast, as well as in squid pens) 13 as additive, it is possible to promote silica polymerization and aggregation in the heterogeneous phase at room temperature, neutral pH and silica concentrations as low as those occurring in sea water or inside the diatom frustules. Our procedural approach leads to bulk biosilica nanoparticles or, alternatively, to similar mesoporous architectures when structural directing agents (SDA) are also added.In order to mimic frustule conditions, 6,14 we have performed the reactions in circulating silica solutions on chitosan flakes blocked in a part of the system in order to favour a certain confining effect (see ESIw). Summarized in Table 1 are the main parameters concerning syntheses of some sel...

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Enzymatic production of biosilica glass using enzymes from sponges: basic aspects and application in nanobiotechnology (material sciences and medicine)

Cited by 79 publications

References 141 publications

Identification of a silicatein(-related) protease in the giant spicules of the deep-sea hexactinellidMonorhaphis chuni

Identification of a silicatein(-related) protease in the giant spicules of the deep-sea hexactinellidMonorhaphis chuni

Recombinant silicateins as model biocatalysts in organosiloxane chemistry

Biomimetic chitosan-mediated synthesis in heterogeneous phase of bulk and mesoporous silica nanoparticles

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