Identification of a new thermostable and alkali-tolerant α-carbonic anhydrase from Lactobacillus delbrueckii as a biocatalyst for CO2 biomineralization

Li, Chun‐Xiu; Jiang, Xiao‐Chen; Yongjuan, Qiu; Xu, Jian‐He

doi:10.1186/s40643-015-0074-4

Cited by 34 publications

(14 citation statements)

References 27 publications

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“…An alkaline pH of 12 causes an activity decrease of approximately 20%, which is similar to that observed in our previous work in the absence of any nitrate [43]. The result is also consistent with Li et al [52], who observe a 50% loss in activity for a bacterial CA once the pH exceeds 6 irrespective of the ionic environment, with this activity stable from pH 8 to 11.0. The relatively small fall in activity also suggests that the LbL coating is still stable under these conditions, as the enzyme is not washed away during the three minute wash of the membrane with water prior to analysis.…”

Section: Effect Of Anions and Toxic Gases On The Activity Of The Immosupporting

confidence: 92%

“…Secondly, it indicates that the enzyme is significantly more thermostable. In prior work, carbonic anhydrase variants isolated from Lactobacillus delbrueckii[52] and the Gossypium hirsutum cotton plant[60] exhibited deactivation energy values of 185 kJ mol -1 and 146 kJ mol -1 , respectively, based on the Wilbur-Anderson activity assay method[61] for CO 2 hydration. Kanbar and Ozdemir[53] obtained values of 120 kJ mol -1 for free BCA and 360 kJ mol -1 for BCA immobilized within a polyurethane foam.…”

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confidence: 99%

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The resilience of carbonic anhydrase enzyme for membrane-based carbon capture applications

Yong

Stevens

Caruso

et al. 2017

International Journal of Greenhouse Gas Control

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A microbial carbonic anhydrase was immobilized onto the surface of hollow fiber membranes to enhance the absorption rate of carbon dioxide into an aqueous 30 wt% potassium carbonate solvent at pH 10-12. The performance of the immobilized enzyme was investigated over long time frames to determine the suitability of this approach for postcombustion carbon capture. The immobilized enzyme was able to maintain activity for up to 80 days at 25°C even when initially exposed to pH 12, however lost activity rapidly when exposed to such high pH at 50°C and subsequently was completely deactivated within 4 days. The effect of sulfur dioxide and nitric oxide that are present in post-combustion flue gas streams was investigated by contacting enzyme immobilized onto flat planar membrane coupons directly with the dry gases and with solutions containing the anions associated with the gases, namely sulfate, sulfite, nitrate and nitrite. The immobilized enzyme maintained at least 80% of its activity even in the presence of 200 mM of these anions or 500 ppm of the dry gases. Our findings indicate that the enzyme is not significantly affected by these toxic gases or their associated anions. Rather, the combination of high pH and ionic strength of the solvent at a high absorption temperature causes a reduction in the enzyme activity and affects the performance of the absorption process.

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Section: Effect Of Anions and Toxic Gases On The Activity Of The Immosupporting

confidence: 92%

mentioning

confidence: 99%

The resilience of carbonic anhydrase enzyme for membrane-based carbon capture applications

Yong

Stevens

Caruso

et al. 2017

International Journal of Greenhouse Gas Control

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“…As list in Table , the k cat and k cat / K m for several different types of CA from Bovine b CA, human h CAI and h CAII, Helicobacter pylori ( Hp CA) and wild type S. yellowstonense ( Ssy CA) are lower than that of Sy CA. Besides, Sy CA has 22,892 WAU/mg is much higher than Ld CA from Lactobacillus delbrueckii (i.e., 454 WAU/mg) . Herein, the heterologous expression of Sy CA by E. coli is after optimization and with higher productivity.…”

Section: Resultsmentioning

confidence: 93%

“…Besides, SyCA has 22,892 WAU/mg is much higher than LdCA from Lactobacillus delbrueckii (i.e., 454 WAU/mg). 34 Herein, the heterologous expression of SyCA by E. coli is after optimization and with higher productivity.…”

Section: Characterization Of Sycamentioning

confidence: 99%

ARduino‐pH Tracker and screening platform for characterization of recombinant carbonic anhydrase in Escherichia coli

Hsu

Tan

Chiu

et al. 2019

Biotechnology Progress

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Carbonic anhydrase (CA, EC 4.2.1.1) is an ancient enzyme with zinc ion as its active site, which catalyzes the chemical reaction of carbon dioxide (CO2) to react with water and form bicarbonate ions. Due to its high catalytic efficiency on CO2 assimilation, CA is expected to use for carbon sequestration in industry. However, the protein expression level, thermostability and high‐throughput screening of an active CA are still with difficulty. In this study, the CA from Sulfurihydrogenibium yellowstonense (denoted as SyCA) was selected for overexpressed in Escherichia coli by different pET vectors. The enzymatic properties including thermo‐stability, pH tolerance, effect of metal ion, and kinetic parameters were characterized through a novel ARduino‐pH Tracker (ART) for monitoring online effectively. The SyCA is thermophilic and acidophilic as it maintains 100% activity at 50°C, while the residual activity is 34.8% after heating at 80°C for 150 min and the optimal pH is 3–5. The kinetic analysis by ART system showed that the k cat/K m of free enzyme was 4.4‐folds that that of whole cell. On the other hand, the screening platforms as Wilbur–Anderson unit, phenol red indicator and size of colony forming unit have been established to explore CA with higher activity. The high‐throughput screening platform is support in direct evolution of CA and further used in the industry.

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“…A similar study was also reported in bacteria from Firmicute phylum. Alkali stable (9.0) and thermostable (50°C) a-CA reported from Lactobacillus delbrueckii is favourable for carbonation and biocalcification (Li et al 2015). The economic feasibility is also essential for the commercialization of technology.…”

Section: Development In Ca-based Mineralization and Phylogenetic Distmentioning

confidence: 99%

Trends, application and future prospectives of microbial carbonic anhydrase mediated carbonation process for CCUS

2017

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Summary Growing industrialization and the desire for a better economy in countries has accelerated the emission of greenhouse gases (GHGs), by more than the buffering capacity of the earth's atmosphere. Among the various GHGs, carbon dioxide occupies the first position in the anthroposphere and has detrimental effects on the ecosystem. For decarbonization, several non‐biological methods of carbon capture, utilization and storage (CCUS) have been in use for the past few decades, but they are suffering from narrow applicability. Recently, CO2 emission and its disposal related problems have encouraged the implementation of bioprocessing to achieve a zero waste economy for a sustainable environment. Microbial carbonic anhydrase (CA) catalyses reversible CO2 hydration and forms metal carbonates that mimic the natural phenomenon of weathering/carbonation and is gaining merit for CCUS. Thus, the diversity and specificity of CAs from different micro‐organisms could be explored for CCUS. In the literature, more than 50 different microbial CAs have been explored for mineral carbonation. Further, microbial CAs can be engineered for the mineral carbonation process to develop new technology. CA driven carbonation is encouraging due to its large storage capacity and favourable chemistry, allowing site‐specific sequestration and reusable product formation for other industries. Moreover, carbonation based CCUS holds five‐fold more sequestration capacity over the next 100 years. Thus, it is an eco‐friendly, feasible, viable option and believed to be the impending technology for CCUS. Here, we attempt to examine the distribution of various types of microbial CAs with their potential applications and future direction for carbon capture. Although there are few key challenges in bio‐based technology, they need to be addressed in order to commercialize the technology.

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Identification of a new thermostable and alkali-tolerant α-carbonic anhydrase from Lactobacillus delbrueckii as a biocatalyst for CO2 biomineralization

Cited by 34 publications

References 27 publications

The resilience of carbonic anhydrase enzyme for membrane-based carbon capture applications

The resilience of carbonic anhydrase enzyme for membrane-based carbon capture applications

ARduino‐pH Tracker and screening platform for characterization of recombinant carbonic anhydrase in Escherichia coli

Trends, application and future prospectives of microbial carbonic anhydrase mediated carbonation process for CCUS

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