Chemical modification of oxalate decarboxylase to improve adsorption capacity

Lin, Rong; He, Junbin; Wu, Jia; Cai, Xinghua; Han, Liang; Liu, Haiqian

doi:10.1016/j.ijbiomac.2017.02.009

Cited by 13 publications

(5 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…126,127 Although the ε-amino group has a greater intrinsic nucleophilicity, the α-amino group can be selectively modified Figure 5. Chemical modification of the Lys amino groups of enzymes using various acid anhydrides, such as acetic anhydride, 141 citraconic anhydride, 143,146 2,3-dichloromaleic anhydride, 137 phthalic anhydride, 148 trimellitic anhydride, 143 pyromellitic anhydride, 142,144,145 and ethylenediaminetetra-acetic dianhydride, 149 resulted in enhanced stability of the biocatalysts through introduction of extra-hydrophilic groups, neutralizing enzymes' cationic nature and switching enzymes' overall charge from positive to negative. through microenvironment control.…”

Section: Lysine and The N-terminusmentioning

confidence: 99%

“…Oxalate decarboxylase (OXDC) decomposes oxalic acid in the treatment of urinary calculi. 149 However, the enzyme preparations are rapidly diluted in the urinary system due to the fluid state of urine. To circumvent this problem, chemical modification of the OXDC was investigated to increase the adsorption capacity of the enzyme onto calcium oxalate crystals thereby enhancing the degradation of oxalate.…”

Section: Lysine and The N-terminusmentioning

confidence: 99%

“…Oxalate decarboxylase (OXDC) decomposes oxalic acid in the treatment of urinary calculi . However, the enzyme preparations are rapidly diluted in the urinary system due to the fluid state of urine.…”

Section: Enzyme Modification With Caasmentioning

confidence: 99%

See 2 more Smart Citations

Recent Advances in Biocatalysis with Chemical Modification and Expanded Amino Acid Alphabet

et al. 2021

View full text Add to dashboard Cite

The two main strategies for enzyme engineering, directed evolution and rational design, have found widespread applications in improving the intrinsic activities of proteins. Although numerous advances have been achieved using these ground-breaking methods, the limited chemical diversity of the biopolymers, restricted to the 20 canonical amino acids, hampers creation of novel enzymes that Nature has never made thus far. To address this, much research has been devoted to expanding the protein sequence space via chemical modifications and/or incorporation of noncanonical amino acids (ncAAs). This review provides a balanced discussion and critical evaluation of the applications, recent advances, and technical breakthroughs in biocatalysis for three approaches: (i) chemical modification of cAAs, (ii) incorporation of ncAAs, and (iii) chemical modification of incorporated ncAAs. Furthermore, the applications of these approaches and the result on the functional properties and mechanistic study of the enzymes are extensively reviewed. We also discuss the design of artificial enzymes and directed evolution strategies for enzymes with ncAAs incorporated. Finally, we discuss the current challenges and future perspectives for biocatalysis using the expanded amino acid alphabet.

show abstract

Section: Lysine and The N-terminusmentioning

confidence: 99%

Section: Lysine and The N-terminusmentioning

confidence: 99%

See 1 more Smart Citation

Recent Advances in Biocatalysis with Chemical Modification and Expanded Amino Acid Alphabet

et al. 2021

View full text Add to dashboard Cite

show abstract

“…The solution pH was adjusted to a range of 2.0 to 7.0, and the relative enzyme activity of Oxdc and mPEG-Oxdc at different pH treatments were measured. The highest activity of the enzyme in the same group was regarded as 100% [32]. Results are shown in Fig.…”

Section: Stability Of Ph Treatmentmentioning

confidence: 99%

Optimization of monomethoxy polyethyleneglycol-modified oxalate decarboxylase by response surface methodology

et al. 2017

Self Cite

View full text Add to dashboard Cite

In order to improve the stability of oxalate decarboxylase (Oxdc), response surface methodology (RSM), based on a four-factor three-level Box-Behnken central composite design was used to optimize the reaction conditions of oxalate decarboxylase (Oxdc) modified with monomethoxy polyethyleneglycol (mPEG5000). Four independent variables such as the ratio of mPEG-aldehyde to Oxdc, reaction time, temperature, and reaction pH were investigated in this work. The structure of modified Oxdc was identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FTIR) spectroscopy, the stability of the modified Oxdc was also investigated. The optimal conditions were as follows: the mole ratio of mPEG-aldehyde to Oxdc of 1:47.6, time of 13.1 h, temperature at 29.9 °C, and the reaction pH of 5.3. Under optimal conditions, experimental modified rate (MR = 73.69%) and recovery rate (RR = 67.58%) were matched well with the predicted value (MR = 75.11%) and (RR = 69.17%). SDS-PAGE and FTIR analysis showed that mPEG was covalently bound to the Oxdc. Compared with native Oxdc, the modified Oxdc (mPEG-Oxdc) showed higher thermal stability and better tolerance to trypsin or different pH treatment. This work will provide a further theoretical reference for enzyme modification and conditional optimization.

show abstract

“…Lactobacillus strains are commonly used in dairy products and medical probiotic formulations due to their efficiency and safety (17)(18)(19)(20). Recently, Campieri et al (21)(22)(23)(24)(25) have found that the oxalate content and stone size were significantly reduced in patients with hyperoxaluria after the Lactobacillus's administration. The degradation of oxalate by Lactobacillus is attributed to the expression of oxalate decarboxylase (OxDC) (26).…”

Section: Introductionmentioning

confidence: 99%

Manipulating Oxalate Decarboxylase Provides the Basis of Antilithic Therapy by Acting on the Gut Microbiota

Cheng

Zhou

et al. 2022

Preprint

View full text Add to dashboard Cite

A high concentration of oxalate is associated with an increased risk of kidney calcium oxalate (CaOx) stones, and the degradation of exogenous oxalate mainly depends on oxalate-degrading enzymes from the intestinal microbiome. We found that Zinc Gluconate supplement to patients with CaOx kidney stones could significantly improve the abundance of oxalate metabolizing bacteria in human body through clinical experiments on the premise of simultaneous antibiotic treatment and the imbalance of Lactobacillus and OxDC was involved in CaOx kidney stones through clinical sample analysis. Then, we identified that Zn2+could be used as an external factor to improve the activity of OxDC and protect Lactobacillus, achieved the preventive effect on rats with stones aggravated by antibiotics. Finally, by analyzing the three-dimensional structure of OxDC and some in vitro experiments, we propose a hypothesis Zn2+increases the metabolism of oxalate in humans through its positive effects on Lactobacillus and OxDC to reduce CaOx kidney stone symptoms in rats.

show abstract

Chemical modification of oxalate decarboxylase to improve adsorption capacity

Cited by 13 publications

References 24 publications

Recent Advances in Biocatalysis with Chemical Modification and Expanded Amino Acid Alphabet

Recent Advances in Biocatalysis with Chemical Modification and Expanded Amino Acid Alphabet

Optimization of monomethoxy polyethyleneglycol-modified oxalate decarboxylase by response surface methodology

Manipulating Oxalate Decarboxylase Provides the Basis of Antilithic Therapy by Acting on the Gut Microbiota

Contact Info

Product

Resources

About