Immobilisation of Candida rugosa lipase on polyhydroxybutyrate via a combination of adsorption and cross-linking agents to enhance acylglycerol production

Binhayeeding, Narisa; Yunu, Tewan; Pichid, Nisa; Klomklao, Sappasith; Sangkharak, Kanokphorn

doi:10.1016/j.procbio.2020.02.007

Cited by 62 publications

(35 citation statements)

References 63 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Previous studies have reached comparable findings indicating that pore size affected the enzymatic loading capacity (Gao et al, 2010). Also, Binhayeeding et al (2020) stated that the resin's modification process also inhibits enzyme adsorption. With adsorptioncrosslinking, the chitosan-coated support showed an admirable result than uncoated support (8.12% higher).…”

Section: Effect Of Amino-functional Group Addition On the Lipase Loadingmentioning

confidence: 86%

Effect of Additional Amino Group to Improve the Performance of Immobilized Lipase From Aspergillus niger by Adsorption-Crosslinking Method

et al. 2021

View full text Add to dashboard Cite

Adsorption-crosslinking is one of the immobilization methods to improve the reusability of lipase. It requires amino groups to reduce cross-link immobilization risk so that lipase–support interaction increases and the immobilization is attainable. Also, the amino group on the support is expected to increase lipase performance. This study aimed to analyze the effect of amino group addition on immobilized Aspergillus niger lipase by the adsorption-crosslinking using MP-64 macroporous anion resin and XAD-7HP macroporous nonionic resin that has been treated with chitosan. The chitosan-coated resin was characterized by Fourier transform infrared spectrometry (FTIR) and scanning electron microscope (SEM). Lipase immobilization was carried out by adding 10 ml lipase solution containing 0.75 g resins and shaken at 25°C for 150 rpm. Adsorption was achieved for 4 h, followed by cross-linking separately (adding 0.5% (v/v) glutaraldehyde and re-reacting for 20 min). Lipase activity was measured with the titrimetric of olive oil emulsion; mixed with Aspergillus niger lipase, emulsion, and a buffer solution (pH 6.5, ionic strength of 0.7); and incubated for 30 min at 37°C. The effect of amino-functional groups was investigated based on lipase loading and lipase activity. The best lipase loading and lipase activity of 83.79% and 29.41 U/g support were achieved in the adsorption-crosslinking using MP-64 resin coated with chitosan. After four cycles, biodiesel synthesis was maintained at 70.61% of the initial yield. These results indicated that chitosan as an affordable and readily available source of amino groups could be used to modify support for Aspergillus niger lipase immobilization.

show abstract

Section: Effect Of Amino-functional Group Addition On the Lipase Loadingmentioning

confidence: 86%

Effect of Additional Amino Group to Improve the Performance of Immobilized Lipase From Aspergillus niger by Adsorption-Crosslinking Method

et al. 2021

View full text Add to dashboard Cite

show abstract

“…The subsequent cross-linking of physical aggregates renders them permanently insoluble while maintaining their activity by maintaining their pre-organized structure [ 129 ]. Binhayeeding et al [ 130 ] used a combination of two immobilization methods to prepare a robust catalyst, such as adsorption followed by cross-linking of the Candida antarctica lipase on an immobilized matrix. Initially, lipase was adsorbed on PHB beads, followed by cross-linking with glutaraldehyde.…”

Section: Enzyme Catalystmentioning

confidence: 99%

Biodiesel Production Using Homogeneous, Heterogeneous, and Enzyme Catalysts via Transesterification and Esterification Reactions: a Critical Review

2021

View full text Add to dashboard Cite

The excessive utilization of petroleum resources leads to global warming, crude oil price fluctuations, and the fast depletion of petroleum reserves. Biodiesel has gained importance over the last few years as a clean, sustainable, and renewable energy source. This review provides knowledge of biodiesel production via transesterification/esterification using different catalysts, their prospects, and their challenges. The intensive research on homogeneous chemical catalysts points to the challenges in using high free fatty acids containing oils, such as waste cooking oils and animal fats. The problems faced are soap formation and the difficulty in product separation. On the other hand, heterogeneous catalysts are more preferable in biodiesel synthesis due to their ease of separation and reusability. However, in-depth studies show the limited activity and selectivity issues. Using biomass waste-based catalysts can reduce the biodiesel production cost as the materials are readily available and cheap. The use of an enzymatic approach has gained precedence in recent times. Additionally, immobilization of these enzymes has also improved the statistics because of their excellent functional properties like easy separation and reusability. However, free/liquid lipases are also growing faster due to better mass transfer with reactants. Biocatalysts are exceptional in good selectivity and mild operational conditions, but attractive features are veiled with the operational costs. Nanocatalysts play a vital role in heterogeneous catalysis and lipase immobilization due to their excellent selectivity, reactivity, faster reaction rates owing to their higher surface area, and easy recovery from the products and reuse for several cycles.

show abstract

“…Considering the pH PZC of CCAC and CCACM at pH 4.0, it is observed that the supports have positive surface charges and the lipase has zero net charge, which shows that hydrophobic interactions between the enzyme and support control the adsorptive process. According to Binhayeeding et al ., 59 near to their isoelectric point enzymes tend to spontaneously form fewer active aggregates and extremes of pH values can cause an irreversible denaturation, which explains the reduction in adsorptive capacity with the increase in immobilization solution pH.…”

Section: Resultsmentioning

confidence: 99%

“…The increase in activity of the derivatives suggests that immobilization on hydrophobic supports prevents conformational changes induced by temperature and, moreover, limits the movement that occurs due to molecular agitation when energy is added to the system. Thus, when the enzyme binds to the support, the susceptibility to thermal denaturation is reduced, allowing for increased stability and higher reaction yields 59,67 …”

Section: Resultsmentioning

confidence: 99%

Incorporation of metallic particles in activated carbon used in lipase immobilization for production of isoamyl acetate

Oliveira

Santos

Brito

et al. 2022

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND: Biotechnology has revolutionized the use of enzymes for application in industrial processes. The present work evaluated the effect of functionalizing activated carbon with metallic nanoparticles obtained from corn cob residue on lipase immobilization. The aim was to improve the enzymatic activity of the immobilized enzyme and subsequent application of derivatives in the synthesis of isoamyl acetate ester (banana flavor). RESULTS:The activated carbon (CCAC) had a mesoporous structure and specific surface area of 1135 m 2 g −1 , characteristic of supports from precursor material with a high cellulose content, which was reduced in metalized carbon (CCACM) due to the insertion of metallic particles (760 m 2 g −1 ). CCACM showed a slightly higher lipase absorptive capacity than CCAC (280.72 ± 0.27 mg g −1 and 276.46 ± 0.03 mg g −1 , respectively). Furthermore, for derivatives the optimal reaction medium conditions were pH 7.0 and 30 °C, confirming the advantage associated with lipase immobilization, obtaining activity values of 84.0 ± 2.12 U, 72.3 ± 1.7 U and 31.4 ± 1.9 U, for lipase immobilized on CCACM, CCAC and native form, respectively. The derivatives showed potential application in the synthesis of isoamyl acetate ester, with conversions above 90% and stability during five cycles of use. CONCLUSION:The activated carbon metallization process showed an increase in lipase immobilization efficiency and proved to be a promising support, since there was an increase in its enzymatic activity and the derivatives obtained showed potential application in aroma synthesis, reaching conversion above 90%.

show abstract

Immobilisation of Candida rugosa lipase on polyhydroxybutyrate via a combination of adsorption and cross-linking agents to enhance acylglycerol production

Cited by 62 publications

References 63 publications

Effect of Additional Amino Group to Improve the Performance of Immobilized Lipase From Aspergillus niger by Adsorption-Crosslinking Method

Effect of Additional Amino Group to Improve the Performance of Immobilized Lipase From Aspergillus niger by Adsorption-Crosslinking Method

Biodiesel Production Using Homogeneous, Heterogeneous, and Enzyme Catalysts via Transesterification and Esterification Reactions: a Critical Review

Incorporation of metallic particles in activated carbon used in lipase immobilization for production of isoamyl acetate

Contact Info

Product

Resources

About