FOOD CHEMISTRY
·
2024
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IF 8.5
Zhong Li,Huilin Zhou,Xuan Liu,Weifei Wang,Dongming Lan,Yonghua Wang
The limited availability of phospholipase A 1 (PLA 1 ) has posed significant challenges in enzymatic degumming. In this study, a novel PLA1 (UM2) was introduced to address this limitation, which had a unique thermo-responsive ability to switch phospholipase and lipase activities in response to temperature variations. Remarkably, UM2 displayed an unprecedented selectivity under optimized conditions, preferentially hydrolyzing phospholipids over triacylglycerols—a specificity superior to that of commercial PLA 1 . Moreover, UM2 demonstrated high efficiency in hydrolyzing phospholipids with a predilection for phosphatidylcholine (PC) and phosphatidylethanolamine (PE). A practical application of UM2 on crude flaxseed oil led to a dramatic reduction in phosphorus content, plummeting from an initial 384.06 mg/kg to 4.38 mg/kg. Broadening its industrial applicability, UM2 effectively performed enzymatic degumming for other distinct crude vegetable oils with a unique phospholipid composition. Collectively, these results highlighted the promising application of UM2 in the field of oil degumming.
研究领域:
生物化学
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食品科学
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DOI
PubMed
高影响因子
JOURNAL OF FOOD SCIENCE AND TECHNOLOGY-MYSORE
·
2021
·Vol. 59
·期 1
·317-326
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IF 2.701
Weining Wang,Tang Honglin,Chen Yan,Liu Jingyang,Yu Dianyu,Yang Fuming,Elfalleh Walid
In this paper, the free Phospholipase A 1 (PLA 1 ) was immobilized on a magnetic carrier. The average particle diameter of the magnetic carrier was 97 ± 1.3 nm, and the average particle diameter of the magnetically immobilized PLA 1 was 105 nm ± 1.3 nm. The enzyme activity was 1940.5 U/g. The magnetic enzyme was chemically modified with formaldehyde, dextran-aldehyde, and dextran-aldehyde-glycine. The proportions of primary amino groups in the modified magnetic immobilized enzyme PLA 1 were 0, 53.5% and 47.3%, respectively. The optimum pH of the enzyme after chemical modification was 6.5. When the system temperature was 60 °C, the magnetically immobilized PLA 1 modified with dextran-aldehyde-glycine had the optimal activity and stability. This chemically modified magnetic immobilized PLA 1 was applied to soybean oil degumming at 60 °C, 6.5 h (reaction time), and 0.10 mg/kg (enzyme dosage). The phosphorus content in the degummed oil was 9.2 mg/kg. The relative enzyme activity was 77.6% after 7 reuses which would be potentially advantageous for industrial applications.
研究领域:
生物化学
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食品科学
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产品关联
DOI
PubMed
高影响因子
Journal of Oleo Science
·
2022
·
IF 1.628
Wenyi Chen,Maomao Kou,Lin Li,Bing Li,Jianrong Huang,Shudong Fan,Li Xu,Nanjing Zhong
In this study, SBA-15 was functionalized by organic groups (-CH3, -C4H9, -C8H17, -CH2CH2NH2, -C6H5, et al.), and then Lecitase® Ultra (LU) was immobilized onto the modified SBA-15 for soybean oil degumming. The hydrolysis activity, degumming performance, reusability in degumming, and the composition of phospholipids in the gum, of the immobilized LU samples, were carefully studied. Hydrolysis activities over 1800 U/g were obtained from all the immobilized LU samples. The highest activity of up to 4554.17 U/g was observed from the 3-ureidopropyl group-modified SBA-15-supported LU. Most of the immobilized LU samples removed the phospholipids effectively from crude soybean oil (initial phosphorous content 314.23 mg/kg), with a residual phosphorus content of less than 10 mg/kg. The reusability of the immobilized LU samples in the degumming process was evaluated. No loss of activity was observed from the methyl and N-(2-aminoethyl)-3-aminopropyl group-modified SBA-15-supported LU samples after five cycles of reuse. In addition, 3-aminopropyl and 3-glycidyloxypropyl group-modified SBA-15-supported LU samples retained over 90% of their initial activity; N-phenylaminomethyl and 1-isocyanatopropane group-functionalized SBA-15-supported LU samples retained approximately 80% of their initial activity. The phospholipids in the gum were analyzed. The n-octadecyl and N-(2-aminoethyl)-3-aminopropyl group-functionalized SBA-15-supported LU samples were selective for lysophosphatidylethanolamine (LPE) preparation, and LPE percentages up to 37.14 and 38.80% were obtained, respectively. The N-phenylaminomethyl group-modified SBA-15-supported LU showed selectivity toward lysophosphatidylcholine (LPC) production, with an LPC percentage of up to 38.5%.
研究领域:
化学工程
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生物化学
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材料科学
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食品科学
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产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2022
·
IF 9.231
Xuan Liu,Weifei Wang,Zexin Zhao,Long Xu,Bo Yang,Dongming Lan,Yonghua Wang
Enzymatic degumming is an essential refining process to improve oil quality. In this study, a monoacylglycerol lipase GMGL was derived from marine Geobacillus sp., and was found that not only took monoacylglycerol (MAG) as substrate, but also had activity toward lysophosphatidylcholine (LPC), lysophosphatidylethanolamine (LPE) and glycerolphosphatidylcholine (GPC). Binding free energy showed LPC and LPE could bind with enzyme stably as MAG. It presented great potential in the field of enzymatic degumming. The phosphorus content in crude soybean oil decreased from 680.50 to 2.01 mg/kg and the yield of oil reached to 98.80 % after treating with phospholipase A1 (Lecitase Ultra) combined with lipase GMGL. An ultrahigh-performance liquid chromatography coupled with quadrupole time-of-flight mass spectrometry (UPLC-Q-TOF-MS) was developed to identify 21 differential phospholipids between crude soybean oil and enzymatic treatment. This work might shed some light on understanding the catalytic mechanism of monoacylglycerol lipase and provide an effective strategy for enzymatic degumming.
研究领域:
食品科学
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酶学
·
脂类化学
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产品关联
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）