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Author

Lixi Cai

Bio: Lixi Cai is an academic researcher from Huaqiao University. The author has contributed to research in topics: Immobilized enzyme & Polysaccharide Hydrolase. The author has an hindex of 1, co-authored 2 publications receiving 3 citations.

Papers
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Journal ArticleDOI
Lixi Cai1, Xin Liu1, Yue Qiu1, Mengqi Liu1, Guangya Zhang1 
TL;DR: This was the first report on the synergy between LPMOs and β-1,3-xylanase, and the strategy for enzyme self-immobilization was simple, timesaving, and efficient, which might have great potentials in algae biomass hydrolysis.
Abstract: Lytic polysaccharide monooxygenases (LPMOs) with synergistic effect on polysaccharide hydrolase represent a revolution in biotechnology, which may accelerate the conversion of biomass to the second-generation biofuels. Discovering more hydrolases that have synergism with LPMOs will considerably expand the knowledge and application of biomass degradation. The LPMOs named CgAA9 were verified to exhibit 1.52-fold synergism when incubated with β-1,3-xylanase at a molar ratio of 3:1. The ion chromatography results proved that CgAA9 did not alter the endogenous hydrolysis mode of β-1,3-xylanase. Meanwhile, to decrease the operational cost of enzymes, a novel strategy for immobilizing LPMOs and β-1,3-xylanases based on the biomimetic silica nanoparticles was developed. It enabled preparation of immobilized enzymes directly from the cell lysate. The immobilization efficiency and activity recovery reached 84.6 and 81.4%. They showed excellent reusability for 12 cycles by retaining 68% of initial activity. The optimum temperature for both free and immobilized biocatalyst were 40 and 37 °C, indicating they were ideal candidates for typical simultaneous saccharification and fermentation (SSF) in ethanol production from algea biomass. This was the first report on the synergy between LPMOs and β-1,3-xylanase, and the strategy for enzyme self-immobilization was simple, timesaving, and efficient, which might have great potentials in algae biomass hydrolysis. • The lytic polysaccharide monooxygenases (LPMOs) from Chaetomium globosum were firstly verified to boost the hydrolysis of β-1,3-xylanases for β-1,3-xylan. • A novel strategy for simple preparation of SpyCather-modifed silica nanopartilcles and intelligent immobilization of target enzymes from the cell lysate was proposed. • The immobilized LPMOs and β-1,3-xylanases could be reasonable alternatives for typical simultaneous saccharification and fermentation (SSF) in manipulation of algae biomass.

9 citations

Journal ArticleDOI
TL;DR: A novel and effective strategy for enzyme immobilization, namely, as elastin-like polypeptide (ELP)-mediated silicification-based protein self-immobilization (ESPSI) is proposed.
Abstract: Recently, we proposed a novel and effective strategy for enzyme immobilization, namely, as elastin-like polypeptide (ELP)-mediated silicification-based protein self-immobilization (ESPSI). Here, an...

7 citations


Cited by
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Xiaokai, Song, Zhongyi, Jiang, Lin, Li, Hong, Wu 
01 Jan 2014
TL;DR: Mesoporous as mentioned in this paper : MESOPorous biomimetic biomimetics is defined as: "a mixture of prehydrolyzed tetraethoxysilane (TEOS) and Glucuronidase (GUS)"
Abstract: Mesoporous 硅石粒子通过一个 biomimetic 矿化作用过程,包含溶解酵素和 GUS 的答案在被增加进 prehydrolyzed tetraethoxysilane (TEOS ) 为 -glucuronidase (GUS ) 的有效固定作好准备答案。硅石粒子在溶解酵素的催化作用下面以 biomineralization 的一个方法被形成, GUS 在降水过程期间同时被使不能调动进硅石粒子。硅石粒子的平均直径是有大约 4 nm 的一种毛孔尺寸的大约 200 nm。没有任何甚至在一个高离子的力量条件下面沥滤,所有酶分子紧在 biosilica nanoparticles 内被骗诱。使不能调动的 GUS 显著地展出更高热并且 pH 稳定性和再循环的稳定性与在免费形式的 GUS 相比。在 30 天的存储,和起始的活动能很好在 12 个重复周期以后被保留以后,在使不能调动的 GUS 的酶活动的损失都没被发现。

20 citations

Journal ArticleDOI
TL;DR: This unique ELP-mediated silicification-based Spy-assisted enzyme self-immobilization (ESSESI) offered great potentials towards multienzyme co-immorphization for diverse applications in a cleaner manner.

17 citations

Journal ArticleDOI
TL;DR: In this paper, the target enzymes were covalently immobilized on silica nanoparticles via elastin-like polypeptides (ELPs)-based biomimetic silicification and SpyTag/SpyCatcher spontaneous reaction.
Abstract: Exploring a simple and versatile technique for direct immobilization of target enzymes from cell lysate without prior purification is urgently needed. Thus, a novel all-in-one strategy for purification and immobilization of β-1,3-xylanase was proposed, the target enzymes were covalently immobilized on silica nanoparticles via elastin-like polypeptides (ELPs)-based biomimetic silicification and SpyTag/SpyCatcher spontaneous reaction. Thus, the functional carriers that did not require the time-consuming surface modification step were quickly and efficiently prepared. These carriers could specifically immobilize the SpyTag-fused target enzymes from the cell lysate without pre-purification. The ELPs-SpyCatcher hardly leaked from the carriers (0.5%), and the immobilization yield of enzyme was up to 96%. Immobilized enzyme retained 85.6% of the initial activity and showed 88.6% of the activity recovery. Compared with free ones, the immobilized β-1,3-xylanase showed improved thermal stability, elevated storage stability and good pH tolerance. It also retained more than 70.6% of initial activity after 12 reaction cycles, demonstrating its excellent reusability. The results clearly highlighted the effectiveness of the novel enzyme immobilization method proposed here due to the improvement of overall performance of immobilized enzyme in respect to free form for the hydrolysis of macromolecular substrates. Thus, it may have great potential in the conversion of algae biomass as well as other related fields.

12 citations

Journal ArticleDOI
TL;DR: In this article , an ELP-tagged self-immobilized cutinase (ET-C) was proposed for polyethylene terephthalate (PET) degradation.

3 citations