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Enzyme-Adsorbed Chitosan Nanogel Particles as Edible Pickering Interfacial Biocatalysts and Lipase-Responsive Phase Inversion of Emulsions

文献类型: 外文期刊

作者: Huang, Xiao-Mei 1 ; Luo, Zhao-Jiao 1 ; Guo, Jian 1 ; Ruan, Qi-Jun 1 ; Wang, Jin-Mei 1 ; Yang, Xiao-quan 1 ;

作者机构: 1.South China Univ Technol, Guangdong Prov Key Lab Green Proc Nat Prod & Prod, Natl Engn Lab Wheat & Corn Further Proc, Prot Res & Dev Ctr, Guangzhou 510640, Guangdong, Peoples R China

2.Guangdong Acad Agr Sci, Sericultural & Agrifood Res Inst, Guangdong Key Lab Agr Prod Proc, Minist Agr & Rural Affairs,Key Lab Funct Foods, Guangzhou 510610, Guangdong, Peoples R China

3.Guangdong Acad Sci, Guangdong Engn & Technol Res Ctr Effect Component, China Natl Analyt Ctr Guangzhou, Guangdong Inst Anal, Guangzhou 510070, Guangdong, Peoples R China

关键词: chitosan nanogel; Pickering biocatalytic emulsion; phase inversion

期刊名称:JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY ( 2020影响因子:5.279; 五年影响因子:5.269 )

ISSN: 0021-8561

年卷期: 2020 年 68 卷 33 期

页码:

收录情况: SCI

摘要: Here, a simple food-grade Pickering emulsion system is prepared and adopted for biphasic biocatalytic reactions. The chitosan nanogels were prepared with strong dispersion of chitosan aggregates approaching neutral pH and then used as the particle emulsifiers to produce oil-in-water Pickering emulsions. The chitosan nanogel exhibited high affinity to negatively charged lipase. As a result of increasing the biphasic interfacial area and loading amount on the oil-water interface, the catalysis activity of lipase and recycling and pH stability were highly enhanced through colorimetric determination of p-nitrophenol (the hydrolysis product of p-nitrophenyl palmitate). A general strategy was proposed to obtain stimulus-responsive Pickering emulsions that can undergo phase inversion. The in situ modification of the wettability of chitosan nanogel could be attributed to the interaction between nanogel and free fatty acids, which was triggered by lipase hydrolysis. This would permit a rapid and controlled release of hydrophobic active components in response to enzymatic triggers.

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