Immobilization of Lipase on Epoxy Activated (1→3)-α-<scp>D</scp>-Glucan Isolated from<i>Penicillium chrysongenum</i>

Wang, Tianqi; Li, Hanxiang; Nie, Kaili; Tan, Tianwei

doi:10.1271/bbb.60292

Cited by 13 publications

(8 citation statements)

References 27 publications

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“…According to the previous report, BGL1 displayed on the yeast cell surface was stable at higher temperatures and pH, compared with secreted BGL1 . Enzymes immobilized on solid supports exhibit increased resistance to inactivation by high temperature and pH (Matsumoto and Kondo 2001;Wang et al 2006). Additionally, immobilization reduces the accessibility of the protein on solid supports to proteolytic cleavage (LiJeune et al 1997).…”

Section: Resultsmentioning

confidence: 99%

“…Displayed enzymes are useful for the production of fuel, some organic acids, etc. Molecular display technology has several advantages: (i) the displayed enzymes are easily separated from products, and are repeatedly used as the catalyst; and, (ii) the displayed enzymes exhibit high reactivity even under severe conditions such as high temperature and extreme pH (Matsumoto and Kondo 2001;Wang et al 2006). Molecular display technology, which increases protein stability, has also been used for the production of oral vaccines (Tamaru et al 2006).…”

Section: Introductionmentioning

confidence: 99%

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Evaluation of cell surface-displayed protein stability against simulated gastric fluid

et al. 2009

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A molecular display technology that uses the displayed proteins on cell surfaces has many applications in microbiology and molecular biology. Here, we describe the resistance of displayed proteins to proteases using simulated gastric fluid (SGF), which included pepsin at pH 2. The displayed beta-glucosidase resisted pepsin digestion compared with secreted, free beta-glucosidase. In SDS-PAGE and Western blotting analysis, the secreted beta-glucosidase was immediately digested within 1 min following SGF treatment, although the displayed beta-glucosidase was stable for more than 60 min following SGF treatment. In addition, the residual activity of secreted beta-glucosidase was completely destroyed after 10 min SGF treatment. However, displayed beta-glucosidase retained 14% of its residual activity following the same treatment. These results clearly show that cell surface display technology using enzymes can reveal the protease resistance of a protein of interest under various conditions.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Evaluation of cell surface-displayed protein stability against simulated gastric fluid

et al. 2009

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“…According to a previous report, BGL1 displayed on the yeast cell surface was stable at higher temperatures and pH, compared with secreted BGL1 [119]. Enzymes immobilized on solid supports exhibit increased resistance to inactivation by high temperature and pH [120,121]. Additionally, immobilization on solid supports reduces the accessibility of the protein to proteolytic cleavage [122].…”

Section: Molecular Display Methods To Study Food Ingredientsmentioning

confidence: 92%

Development of Yeast Molecular Display Systems Focused on Therapeutic Proteins, Enzymes, and Foods: Functional Analysis of Proteins and its Application to Bioconversion

Shibasaki

Ueda²

2010

BIOT

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Molecular display systems using yeast have been developed for industrial, medical, pharmaceutical, and biological studies. Although several host cells are available to construct a molecular display system, the yeast Saccharomyces cerevisiae is a well-established and convenient organism in eukaryotes. A wide variety of prokaryotic and eukaryotic proteins have been displayed on yeast cell surfaces. In addition, functional analyses and applications to bioconversion have been performed on the cell surface, and cells are conveniently engineered by molecular display systems. In this review, we focus on the yeast molecular display system with regard to therapeutic proteins, several enzymes, and food ingredients. In addition, recent patents on molecular display using yeast cell for production of those compounds, screening technology and related techniques are introduced. Development of devices for functional analysis of created and modified proteins in the yeast display system is also described.

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“…Due to its insolubility in water, (1→3)-α-d-glucan from Penicillium chrysogenum mycelia was a substrate for the preparation of epoxyactivated microsphere as carrier for efficient immobilization of lipase derived from Candida sp. [7].…”

Section: Digital Signaturementioning

confidence: 99%

Fruiting bodies of Hericium erinaceus (Bull.) Pers. – a new source of water-insoluble (1→3)-α-d-glucan

et al. 2016

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A water-insoluble polysaccharide (WIP) was isolated from the fruiting bodies of Hericium erinaceus HE01 by an alkaline solution with the yield of 5%. Structural and compositional analyses by total acid hydrolysis, methylation analysis, FT-IR, FT-Raman, and 1 H NMR spectroscopy as well as other instrumental techniques showed predominantly glucose linked by α-glycosidic bonds and small amounts of mannose, xylose, rhamnose, galactose, and ribose. The methylation analysis showed that (1→3)-linked Glcp is the major constituent (70.8%) of the polymer, while the 3,4 substituted d-Glcp represents the main branching residue of the glucan. The presence of (1→3)-α-d-glucan in the hyphae of H. erinaceus was additionally confirmed by the use of specific fluorophore-labeled antibodies.

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Immobilization of Lipase on Epoxy Activated (1→3)-α-D-Glucan Isolated fromPenicillium chrysongenum

Cited by 13 publications

References 27 publications

Evaluation of cell surface-displayed protein stability against simulated gastric fluid

Evaluation of cell surface-displayed protein stability against simulated gastric fluid

Development of Yeast Molecular Display Systems Focused on Therapeutic Proteins, Enzymes, and Foods: Functional Analysis of Proteins and its Application to Bioconversion

Fruiting bodies of Hericium erinaceus (Bull.) Pers. – a new source of water-insoluble (1→3)-α-d-glucan

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