Biofabrication of gold nanoparticles by Shewanella species

Wu, Jhe Wei; Ng, I-Son

doi:10.1186/s40643-017-0181-5

Cited by 25 publications

(20 citation statements)

References 43 publications

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“…Moreover, the hybrid organic-inorganic character of certain MOFs seems to favor the interaction of these materials with enzymes, since solid active biocatalysts can be formed by just contacting both species, even when the material does not contain enough large pores to host the enzyme [11]. Very different approaches to immobilize enzymes (more generally, proteins) on/in MOF materials have been recently developed and published elsewhere [26][27][28][29][30][31][32][33][34][35][36][37][38][39][40][41][42][43][44][45]. Some of them are based on the co-precipitation of the enzyme and the MOF material [26,28,29,[40][41][42][43][44] The exponential increase of the number of papers of enzyme@MOF biocatalysts certifies, on the one hand, the enormous interest of the scientific community in this subject and, on the other hand, the very favorable physicochemical interaction between MOF supports and the proteins.…”

Section: Introductionmentioning

confidence: 99%

Semi-crystalline Fe-BTC MOF material as an efficient support for enzyme immobilization

et al. 2018

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Graphical abstractResearch Highlights: Semi-crystalline Fe-BTC MOF material is an efficient support for enzymes  It can be used by either in-situ or post-synthesis approaches  The in-situ (one-step) biocatalysts are more active and have lower enzyme leaching  This enzyme support improves the benefits given by some other MOF-based supports ABSTRACT. Metal-organic frameworks (MOFs) have revolutionized the potential applications of nanoporous materials. One of the most recent and promising applications of these materials is their use as supports for enzyme immobilization. In this context, the in-situ (one-step) methodologies, which do not require the use of MOFs with pores larger than the enzyme to be immobilized, seem to be particularly encouraging. This work presents a systematic study of the semi-crystalline Fe-BTC MOF material (commercialized as Basolite F300) employed as support of the enzymes laccase and lipase through either in-situ or postsynthesis methodology. The presence of the enzyme in the resultant solid biocatalysts was proved by CHNS chemical analysis, thermogravimetric analysis, Bradford assays and by SDS-PAGE electrophoresis. The enzymatic activity of the resultant Fe-BTC-based biocatalysts was also tested. The in-situ approach is particularly relevant due to various reasons: (i) the enzyme immobilization is given in one step; (ii) it is rapid (10 minutes); (iii) it is very efficient in terms of encapsulation capacity (≥ 98 % for laccase and ≥ 87 % for lipase); (iv) the enzymes are fully retained and no leaching is observed after an initial release of only around 10% of the enzyme molecules weakly immobilized; and (v) the activity of the retained enzyme can be substantially maintained (97 % with respect to the free enzyme in the case of lipase). Any of these parameters systematically improves these given by the post-synthesis (two-step) approach. Moreover, Fe-BTC widely surpasses the benefits given by other MOF-based supports either by in-situ or postsynthesis approaches.

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Section: Introductionmentioning

confidence: 99%

Semi-crystalline Fe-BTC MOF material as an efficient support for enzyme immobilization

et al. 2018

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“…[20] Also, a similar report suggested immobilization of lipase, HRP (horseradish peroxidase), and catalase into ZIF-10, ZIF-8, and ZIF-90, respectively. [21] Further, researchers also have immobilized multiple enzymes within a ZIF-8 composite. [22] More recently, in situ synthesis of glucoamylase metal-organic framework was reported by a similar facile one-pot synthesis strategy.…”

Section: Introductionmentioning

confidence: 99%

Rapid In Situ Encapsulation of Laccase into Metal‐Organic Framework Support (ZIF‐8) under Biocompatible Conditions

Patil

Yadav

2018

ChemistrySelect

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In situ immobilization of laccase into metal‐organic framework (laccase‐MOF) was performed by assisting one‐pot synthesis strategy. A novel method to synthesize octahedral laccase‐MOF composite with enhanced thermostability is reported. The present work deals with entrapment of laccase into zeolitic imidazolate framework (ZIF‐8) by simply mixing solution of zinc acetate, 2‐methylimidazole, and laccase at room temperature (28 ± 2 °C). Fourier transform‐infrared spectroscopy (FT‐IR), Scanning electron microscopy (SEM), Thermogravimetric analysis (TGA), and Confocal scanning microscopy were employed to characterize laccase‐MOF composite. The thermostability of prepared composite was assessed concerning half‐life at varying temperatures which conferred 3.6‐fold enhancement over free enzyme. Also, kinetic studies of immobilized laccase showed a slightly higher Km and lower Vmax values along with the enhancement of thermodynamic parameters after non‐covalent interaction. Moreover, the immobilized laccase‐MOF maintained up to 48% of residual activity for seven subsequent cycles in batch mode, whereas the storage stability studies exhibited up to 83% up to 21 days of storage. Finally, FT‐IR data tool was employed to investigate the effect of encapsulation on fractions of secondary structure of protein.

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“…[8][9][10][11][12][13][14][15][16][17] In this regard, enzyme-inorganic techniques such as conjugation, cross-linking and self-assembly hybrid nanomaterials produced by a variety of immobilization have received a significant attention because of their effectiveness to retain and stabilize enzyme activity. [18][19][20][21][22][23][24] Ge et al reported an innovative strategy to synthesize hybrid nanostructures having flower-like shapes (nanoflowers) based on the combination of enzyme molecules with metal salts in phosphate buffer. [25,26] The hybrid nanoflowers were more active and stable than conventionally immobilized enzymes owing to their large surface area and effective confinement of enzyme molecules in their core.…”

Section: Introductionmentioning

confidence: 99%

An Ultrafast Sonochemical Strategy to Synthesize Lipase‐Manganese Phosphate Hybrid Nanoflowers with Promoted Biocatalytic Performance in the Kinetic Resolution of β‐Aryloxyalcohols

2018

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Herein we report an expeditious and facile sonochemical synthesis method that takes just a few minutes to produce organic‐inorganic hybrid nanoflowers and their application as a nanobiocatalyst. Surfactant treated Burkholderia cepacia lipase was used as the organic component and manganese sulfate as the inorganic component to synthesize the nanoflowers in less than 10 minutes. Careful investigation of the process parameters was performed to obtain the optimized value for each attribute viz. sonication time (7.5 min), lipase concentration (0.1 mg/mL), MnSO4 concentration (150 mM), sonication frequency (33 kHz) and pH (8.0). An additional post‐synthesis treatment of nanoflowers with N‐hydroxysuccinimide (NHS) increased their reusability to over nine cycles with an overall six‐fold increase in the activity. In addition, thermal stability was demonstrated through a twenty‐fold increase in the half‐life of immobilized lipase at 80 °C than in free form. The hybrid nanoflowers displayed a marked improvement in the kinetic resolution of racemic intermediates of metoprolol, a selective β‐1 blocker drug [C (%)=46.7, eep=96.5, E=156] and cloranolol, a non‐selective β‐blocker drug [C (%)=49.5, eep=96.0, E=157] compared to free lipase which signifies its importance as a nanobiocatalyst.

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Biofabrication of gold nanoparticles by Shewanella species

Cited by 25 publications

References 43 publications

Semi-crystalline Fe-BTC MOF material as an efficient support for enzyme immobilization

Semi-crystalline Fe-BTC MOF material as an efficient support for enzyme immobilization

Rapid In Situ Encapsulation of Laccase into Metal‐Organic Framework Support (ZIF‐8) under Biocompatible Conditions

An Ultrafast Sonochemical Strategy to Synthesize Lipase‐Manganese Phosphate Hybrid Nanoflowers with Promoted Biocatalytic Performance in the Kinetic Resolution of β‐Aryloxyalcohols

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