Stability of Soybean Oil Degumming Using Immobilized Phospholipase A2

Yu, Dianyu; Ma, Xiaoxing; Jiang, Lianzhou; Elfalleh, Walid; He, Shenghua; He, Yanming; Zhou, Xiaoyu; Zhang, Jianing; Hu, Lizhi

doi:10.5650/jos.ess13105

Cited by 12 publications

(10 citation statements)

References 21 publications

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“…Compared to Wa-PLA 2 –CA beads, the residual activities of CAG–Wa-PLA 2 -I/CAG–Wa-PLA 2 -II and CAC–Wa-PLA 2 -I/CAC–Wa-PLA 2 -II were remarkably increased by about 22 and 30%, respectively. Actually, the incorporation of gelatin into sodium alginate has been reported to highly improve the retention of both PLA 1 and PLA 2 activities. , Similarly, more than 80% retention of PLA 1 activity was noticed in hydrogel incorporating gelatin (43.5%) cross-linked with glutaraldehyde . Therefore, one could conclude that using CA alone as the substrate for the immobilization of both Wa-PLA 2 -I and Wa-PLA 2 -II does not result in a perfect product.…”

Section: Resultsmentioning

confidence: 99%

“…The authors reported that about 32% of diacylglycerol might be produced even after 28 glycerolysis reaction runs. Interestingly, at 55 °C, PLA 1 immobilized on magnetic nanoparticles exhibited more than 80% of its initial activity even after 10 runs of soybean oil degumming reaction …”

Section: Resultsmentioning

confidence: 99%

“…Numerous methods have been described for enzyme immobilization, including cross-linking with glutaraldehyde, covalent attachment on gelatin and chitosan, entrapment in calcium alginate, or a combination of these techniques. ,, …”

Section: Introductionmentioning

confidence: 99%

“…17 Numerous methods have been described for enzyme immobilization, including cross-linking with glutaraldehyde, covalent attachment on gelatin and chitosan, entrapment in calcium alginate, or a combination of these techniques. 9,18,19 In general, immobilization through adsorption or entrapment contributes to maintaining the catalytic activity of enzymes. However, cross-linking and covalent bonding techniques are effective in preserving stability.…”

Section: Introductionmentioning

confidence: 99%

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Effective Soybean Oil Degumming by Immobilized Phospholipases A₂ from Walterinnesia aegyptia Venom

Bacha,

Alonazi

2024

ACS Omega

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Enzymatic degumming utilizing phospholipase enzymes could be used in ecologically friendly procedures with enhanced oil recovery yields. In this study, two phospholipases A 2 of group I and II, WaPLA 2 -I and WaPLA 2 -II, from the snake venom of Saudi Walterinnesia aegyptia were evaluated for soybean oil degumming after being immobilized on three different support materials (calcium alginate (CA), CA-gelatin (CAG), and CA-chitosan (CAC), and cross-linked with glutaraldehyde). Higher yields of CAC-immobilized PLA 2 -I (85 ± 3%) and PLA 2 -II (87 ± 3.6%) compared to CAG (77.3 ± 2.1 and 79 ± 2.6%, respectively) and CA beads (55.7 ± 2.5% and 57.3 ± 3.1%, respectively) were observed. In addition, the optimal temperature of immobilized WaPLA 2 -I and WaPLA 2 -II increased from 45 to 55 °C and from 55 to 65 °C, respectively. Their stability at high temperatures was also significantly enhanced covering a larger range (70−80 °C). Likewise, the pH/activity profile of WaPLA 2 was greatly expanded upon immobilization with the pH-optima being shifted by 0.5 to 1 pH unit to the basic side. Similarly, the stability of WaPLA 2 s in the presence of organic solvents was also significantly improved, while the affinity for calcium and bile salt was the same for both free and immobilized enzymes. Interestingly, the remaining activity of immobilized WaPLA 2 onto different supports was more than 50 or 60% after eight recycles or 120 days of storage at 4 °C, respectively. CAC−WaPLA 2 -II was the best immobilized enzyme complex for the oil degumming process by reducing its final residual phosphorus content from 168 mg/kg to less than 10 mg/kg in only 4 h. Overall, CAC− WaPLA 2 -II showed the most attractive profiles of temperature, pH, and reaction duration as well as significant storage stability and reusability.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effective Soybean Oil Degumming by Immobilized Phospholipases A₂ from Walterinnesia aegyptia Venom

Bacha,

Alonazi

2024

ACS Omega

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“…ese drawbacks can generally be overcome by immobilization. e immobilization of free enzyme improves its tolerance, stability, and easy separation from the product, and realizes the recovery and reuse of the enzyme [7]. Enzyme immobilization methods mainly include entrapping, adsorption, covalent bonding, and cross-linking methods.…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Application of Nanomagnetic Immobilized Phospholipase C

Jiang

Tang

et al. 2019

Journal of Chemistry

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The nanomagnetic carrier (Fe3O4@SiO2@p(GMA)) was prepared by atom transfer radical polymerization, and then, the free phospholipase C (PLC) was immobilized on it proved by the results of FT-IR analysis. The enzyme loading was 135.64 mg/g, the enzyme activity was 8560.7 U/g, the average particle size was 99.86 ± 0.80 nm, and the specific saturation magnetization was 16.00 ± 0.20 emu/g. PLC-Fe3O4@SiO2@p(GMA) showed the highest activities at the pH of 7.5, and tolerance temperature raised to 65°C in soybean lecithin emulsion. Enzymatic degumming with PLC-Fe3O4@SiO2@p(GMA) under the conditions of the enzyme dosage of 110 mg/kg, reaction temperature of 65°C, pH of 7.5, and reaction time of 2.5 h resulted in residual phosphorus of 64.7 mg/kg, 1,2-diacylglycerol (1,2-DAG) contents of 1.07%, and oil yield of 98.1%. Moreover, PLC-Fe3O4@SiO2@p(GMA) still possessed more than 80% of its initial activity after 5 cycles.

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Characterization of a novel thermophilic phospholipase B from Thermotoga lettingae TMO: applicability in enzymatic degumming of vegetable oils

Wei

Xuan

et al. 2015

Journal of Industrial Microbiology and Biotechnology

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A novel phospholipase B (TLPLB) from Thermotoga lettingae TMO has been cloned, functionally overexpressed in Escherichia coli and purified to homogeneity. Gas chromatography indicated that the enzyme could efficiently hydrolyze both the sn-1 and sn-2 ester bonds of 1-palmitoyl-2-oleoyl phosphatidylcholine as phospholipase B. TLPLB was optimally active at 70 °C and pH 5.5, respectively. Its thermostability is relatively high with a half-life of 240 min at 90 °C. TLPLB also displayed remarkable organic solvent tolerance and maintained approximately 91-161 % of its initial activity in 20 and 50 % (v/v) hydrophobic organic solvents after incubation for 168 h. Furthermore, TLPLB exhibited high degumming activity towards rapeseed, soybean, peanut and sunflower seed oils, where the phosphorus contents were decreased from 225.2, 189.3, 85.6 and 70.4 mg/kg to 4.9, 4.7, 3.2 and 2.2 mg/kg within 5 h, respectively. TLPLB could therefore be used for the degumming of vegetable oils.

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Stability of Soybean Oil Degumming Using Immobilized Phospholipase A2

Cited by 12 publications

References 21 publications

Effective Soybean Oil Degumming by Immobilized Phospholipases A₂ from Walterinnesia aegyptia Venom

Effective Soybean Oil Degumming by Immobilized Phospholipases A₂ from Walterinnesia aegyptia Venom

Synthesis and Application of Nanomagnetic Immobilized Phospholipase C

Characterization of a novel thermophilic phospholipase B from Thermotoga lettingae TMO: applicability in enzymatic degumming of vegetable oils

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Stability of Soybean Oil Degumming Using Immobilized Phospholipase A2

Cited by 12 publications

References 21 publications

Effective Soybean Oil Degumming by Immobilized Phospholipases A2 from Walterinnesia aegyptia Venom

Effective Soybean Oil Degumming by Immobilized Phospholipases A2 from Walterinnesia aegyptia Venom

Synthesis and Application of Nanomagnetic Immobilized Phospholipase C

Characterization of a novel thermophilic phospholipase B from Thermotoga lettingae TMO: applicability in enzymatic degumming of vegetable oils

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Effective Soybean Oil Degumming by Immobilized Phospholipases A₂ from Walterinnesia aegyptia Venom

Effective Soybean Oil Degumming by Immobilized Phospholipases A₂ from Walterinnesia aegyptia Venom