Enhancement of lipase stability and productivity through chemical modification and its application to latex-based polymer emulsions

Jayawardena, Menuk B.; Yee, Lachlan H; Poljak, Anne; Cavicchioli, Ricardo; Kjelleberg, Staffan J; Siddiqui, Khawar Sohail

doi:10.1016/j.procbio.2017.03.014

Cited by 18 publications

(15 citation statements)

References 65 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The above results show that the half-life of the enzyme which is a factor of the enzyme stability, in this case under high temperatures, was remarkably increased following the modification using CA and MA. Modification of lipase with ficoll, benzoic anhydride and polyethylene glycol improved the half-lives of thermal inactivation for all modified variants from 40 to 166% at 50, 60 and 70 °C relative to unmodified lipases [ 13 ]. More dramatic increase in half-life was observed in the current experiment for both CA and MA modified amylase enzymes.…”

Section: Resultsmentioning

confidence: 99%

“…The lysine molecules on the amylase surface are very reactive and do not play any role in its activity. It is on the ϵ-amino groups of these lysine molecules that the carboxylic groups from the anhydrides are attached [ 13 ]. Since more than half of the residues adjacent to the lysine molecules are hydrophobic amino acids [ 14 ], attachment of the bulky carboxylic groups masks the non-polar hydrophobic residues, thereby protecting them from unfavorable interactions with the aqueous environment and further stabilizing the enzyme structure.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Citraconylation and maleylation on the catalytic and thermodynamic properties of raw starch saccharifying amylase from Aspergillus carbonarius

Nwagu

Aoyagi

Okolo

et al. 2020

Heliyon

View full text Add to dashboard Cite

Amylase capable of raw starch digestion presents a cheap and easier means of reducing sugar generation from various starch sources. Unfortunately, its potential for use in numerous industrial processes is hindered by poor stability. In this work, chemical modification by acylation using citraconic anhydride (CA) and maleic anhydride (MA) was used to stabilize the raw starch saccharifying amylase from A. carbonarius . The effect of the anhydrides on the pH and thermal stability of the free amylase was investigated. Enzyme kinetics and thermodynamic studies of the free and modified amylase were also carried out. Blue shifts in fluorescent spectra were observed after modification with both anhydrides. Citraconylation led to increased affinity of the enzyme for raw potato starch, unlike maleylation. The activation energy (kJ mol −1 ) for enzyme inactivation was increased by 94.8% after modification with CA while only 17.9% increase was noted after modification with MA. Acylation led to an increase in Gibb's free energy and enthalpy while a reduction in entropy was observed. At 80 °C the half-life (h) was 5.92, 11.18 and 14.74 for free, MA and CA enzyme samples, respectively. These findings have potential value in all industries interested in starch conversion to sugars.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Citraconylation and maleylation on the catalytic and thermodynamic properties of raw starch saccharifying amylase from Aspergillus carbonarius

Nwagu

Aoyagi

Okolo

et al. 2020

Heliyon

View full text Add to dashboard Cite

show abstract

“…The chemical modifications targeting the amino residues of the microbial enzymes have been shown to be effective in delaying their rapid rate of inactivation in the paint. 63 Fungi produce extracellular enzymes according to the chemical composition of the substrates they consume for growth. Moreover, secretions of hydrolytic enzymes as lipases and urease have been recognized as a main virulence factor of diseases by human pathogenic microorganisms.…”

Section: Discussionmentioning

confidence: 99%

Fungi-induced paint deterioration and air contamination in the Assiut University hospital, Egypt

Abdel-Rahim

Nafady

Bagy

et al. 2018

Indoor and Built Environment

View full text Add to dashboard Cite

This study aims to evaluate the correlation between fungi causing paint deterioration and air contamination in Assiut University hospital to give a complete picture for the fungal quantity and spectrum. Seventeen fungal species were isolated from 15 samples of deteriorated water-based paint collected from the hospitals. Chaetomium globosum was the most common paint-deteriorating fungal species, followed by Alternaria alternata, Aspergillus parasiticus, Penicillium oxalicum and Setosphaeria rostrata. Direct examination confirmed the ability of these fungi to colonize the paint samples producing mycelia, conidia and fruiting bodies. In vitro, these fungi exhibited high potential to utilize the thin layer of polyacrylic paint and significant enzymatic activities of cellulase, lipase and urease that may play a main role in paint degradation and as virulence factor of human diseases. Moreover, 27 fungal species were isolated as air contaminating mycobiota. Aspergillus spp., Cladosporium cladosporioides, P. oxalicum, A. alternata and C. globosum caused a considerable amount of indoor air contamination. The results indicated that there is a clear correlation between fungi causing paint deterioration and air contamination, whereas certain fungi were responsible for wall paint deterioration and frequently indoor air contamination. The current study suggests that improvement of antimicrobial additives of paints may be a promising approach to reduce paint biodeterioration and subsequently air contamination of indoor environments.

show abstract

“…Higher productivities of all lipases were due to their higher protein stability and resistance to thermal unfolding at higher temperature. Moreover, the modified lipases retained better activity in paint emulsions after 20 weeks of incubation at 25 • C, indicating that they may have a potentially superior value for industrial applications [18].…”

Section: Higher Productivity Due To Chemical Modificationmentioning

confidence: 99%

Evaluating Enzymatic Productivity—The Missing Link to Enzyme Utility

Siddiqui

Ertan

Poljak

et al. 2022

IJMS

Self Cite

View full text Add to dashboard Cite

Kinetic productivity analysis is critical to the characterization of enzyme catalytic performance and capacity. However, productivity analysis has been largely overlooked in the published literature. Less than 0.01% of studies which report on enzyme characterization present productivity analysis, despite the fact that this is the only measurement method that provides a reliable indicator of potential commercial utility. Here, we argue that reporting productivity data involving native, modified, and immobilized enzymes under different reaction conditions will be of immense value in optimizing enzymatic processes, with a view to accelerating biotechnological applications. With the use of examples from wide-ranging studies, we demonstrate that productivity is a measure of critical importance to the translational and commercial use of enzymes and processes that employ them. We conclude the review by suggesting steps to maximize the productivity of enzyme catalyzed reactions.

show abstract

Enhancement of lipase stability and productivity through chemical modification and its application to latex-based polymer emulsions

Cited by 18 publications

References 65 publications

Citraconylation and maleylation on the catalytic and thermodynamic properties of raw starch saccharifying amylase from Aspergillus carbonarius

Citraconylation and maleylation on the catalytic and thermodynamic properties of raw starch saccharifying amylase from Aspergillus carbonarius

Fungi-induced paint deterioration and air contamination in the Assiut University hospital, Egypt

Evaluating Enzymatic Productivity—The Missing Link to Enzyme Utility

Contact Info

Product

Resources

About