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Shuang Zhang,Wenting Shang,Xiaoxi Yang,Shujuan Zhang,Xiaogang Zhang,Jiawei Chen 대한화학회 2013 Bulletin of the Korean Chemical Society Vol.34 No.9
The immobilization of enzyme is one of the key issues both in the field of enzymatic research and industrialization. In this work, we reported a facile method to immobilize Candida Antarctica lipase B (CALB) in alginate carrier. In the presence of calcium cation, the enzyme-alginate suspension could be cross-linked to form beads with porous structure at room temperature, and the enzyme CALB was dispersed in the beads. Activity of the enzyme-alginate composite was verified by enzymatic hydrolysis reaction of p-nitrophenol butyrate in aqueous phase. The effects of reaction parameters such as temperature, pH, embedding and lyophilized time on the reactive behavior were discussed. Reuse cycle experiments for the hydrolysis of pnitrophenol butyrate demonstrated that activity of the enzyme-alginate composite was maintained without marked deactivation up to 6 repeated cycles.
Zhang, Shuang,Shang, Wenting,Yang, Xiaoxi,Zhang, Shujuan,Zhang, Xiaogang,Chen, Jiawei Korean Chemical Society 2013 Bulletin of the Korean Chemical Society Vol.34 No.9
The immobilization of enzyme is one of the key issues both in the field of enzymatic research and industrialization. In this work, we reported a facile method to immobilize Candida Antarctica lipase B (CALB) in alginate carrier. In the presence of calcium cation, the enzyme-alginate suspension could be cross-linked to form beads with porous structure at room temperature, and the enzyme CALB was dispersed in the beads. Activity of the enzyme-alginate composite was verified by enzymatic hydrolysis reaction of p-nitrophenol butyrate in aqueous phase. The effects of reaction parameters such as temperature, pH, embedding and lyophilized time on the reactive behavior were discussed. Reuse cycle experiments for the hydrolysis of p-nitrophenol butyrate demonstrated that activity of the enzyme-alginate composite was maintained without marked deactivation up to 6 repeated cycles.
Rui Yang,Yuqian Liu,Jingjing Xu,Wenting Shang,Xiaoyuan Zhang,Yongjin Wang,Chris Blanchard,Zhongkai Zhou 한국식품과학회 2018 Food Science and Biotechnology Vol.27 No.6
Epigallocatechin gallate (EGCG) is sensitive to heat thus its application in food industry is limited. In this work, rice bran albumin protein (RAP) was used as a carrier for EGCG. RAP-EGCG complexes (RAPE) were prepared with the binding number n of 0.0505:1 (EGCG: RAP, w/w) and binding constant K of (0.74 ± 0.002) 9 104 M-1, which suggests that hydrogen bond/van der Waals forces played important roles in such binding. FTIR analysis demonstrated that EGCG could induce the secondary structure changes of RAP above the ratio of 1.92:1 (EGCG:RAP, w/w). Dynamic light scattering and scanning electron microscope results showed that EGCG could trigger RAP association. Furthermore, the EGCG stability in RAPE was significantly improved than that of free EGCG in 10–60 C. The antioxidant ability of EGCG in RAPE was partially retained. These findings prove that RAP is a potential carrier for polyphenols and is beneficial for mechanism investigation between protein and polyphenols.