Enzymatic synthesis of amylose

Ohdan, Kohji; Fujii, Kazutoshi; Yanase, Michiyo; Takaha, Takeshi; Kuriki, Takashi

doi:10.1080/10242420600598152

Cited by 100 publications

(61 citation statements)

References 17 publications

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“…The type of cross-linking structure often determines properties of the hydrogels. Because amylose can enzymatically be prepared and hydrolyzed by the phosphorylase and amylase catalyses, respectively [17][18][19][20][21][22]49], hydrogels with cross-linking structures based on amylose have a possibility for enzymatic disruption and reproduction behaviors by two enzyme-catalyzed reactions, i.e., the amylase-catalyzed hydrolysis of amylose and the formation of amylose by the phosphorylase-catalyzed polymerization. Therefore, the preparation of hydrogels through the formation of inclusion complexes of amylose in the vine-twining polymerization was investigated [50].…”

Section: Preparation Of Hydrogels Through Formation Of Inclusion Compmentioning

confidence: 99%

“…In the glycosylation, a glucose unit is transferred from G-1-P to a non-reducing end of the primer to form α-(14)-glycosidic linkage. When the excess molar ratio of G-1-P to the primer is present in the reaction system, the successive glycosylations occur as a propagation of polymerization to produce the α-(14)-glucan chain, i.e., amylose [17][18][19][20][21][22]. Because the phosphorylase-catalyzed polymerization proceeds analogously to a living polymerization, the molecular weight of the produced amylose has a narrow distribution (M w /M n < 1.2) and can be controlled by the G-1-P/primer feed molar ratios [4].…”

Section: Introductionmentioning

confidence: 99%

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Preparation and Applications of Amylose Supramolecules by Means of Phosphorylase-Catalyzed Enzymatic Polymerization

Kadokawa

2012

Polymers

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This paper reviews preparation and applications of amylose supramolecules by means of phosphorylase-catalyzed enzymatic polymerization. When the enzymatic polymerization of α-D-glucose 1-phosphate (G-1-P) as a monomer was carried out in the presence of poly(tetrahydrofuran) (PTHF) of a hydrophobic polyether as a guest polymer, the supramolecule, i.e., an amylose-PTHF inclusion complex, was formed in the process of polymerization. Because the representation of propagation in the polymerization is similar to the way that vines of plants grow twining around rods, this polymerization method for the preparation of amylose-polymer inclusion complexes was proposed to be named -vine-twining polymerization‖. Various hydrophobic polyethers, polyesters, poly(ester-ether), and polycarbonates were also employed as the guest polymer in the vine-twining polymerization to produce the corresponding inclusion complexes. To obtain the inclusion complex from a strongly hydrophobic guest polymer, the parallel enzymatic polymerization system was developed as an advanced extension of the vine-twining polymerization. In addition, it was found that amylose selectively includes one side of the guest polymer from a mixture of two resemblant guest polymers, as well as a specific range in molecular weights of the guest PTHF. Amylose also exhibited selective inclusion behavior toward stereoisomers of poly(lactide)s. Moreover, the preparation of hydrogels through the formation of inclusion complexes of amylose in vine-twining polymerization was achieved.

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Section: Preparation Of Hydrogels Through Formation Of Inclusion Compmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Preparation and Applications of Amylose Supramolecules by Means of Phosphorylase-Catalyzed Enzymatic Polymerization

Kadokawa

2012

Polymers

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“…UDP-glucose, a natural substrate for in vivo glycogen synthesis, was also used as substrate by using glycogen synthase and BE as catalysts (Parodi et al 1969). Although both G-1-P and UDP-glucose are expensive for industrial applications, the former could be obtained from the inexpensive substrate sucrose by using sucrose phosphorylase (SP, EC 2.4.1.7) (SP-GP-BE method) (Ohdan et al 2006). Furthermore, we have demonstrated that ESG produced by the SP-GP-BE method has immunomodulating activity (Ryoyama et al 2004).…”

Section: In Vitro Synthesis Of Glycogenmentioning

confidence: 99%

In vitro synthesis of glycogen: the structure, properties, and physiological function of enzymatically-synthesized glycogen

et al. 2011

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This review describes a new enzymatic method for in vitro glycogen synthesis and its structure and properties. In this method, short-chain amylose is used as the substrate for branching enzymes (BE, EC 2.4.1.18). Although a kidney bean BE and Bacillus cereus BE could not synthesize high-molecular weight glucan, BEs from 6 other bacterial sources produced enzymatically synthesized glycogen (ESG). The BE from Aquifex aeolicus was the most suitable for the production of glycogen with a weight-average molecular weight (Mw) of 3,000-30,000 k. The molecular weight of the ESG is controllable by changing the concentration of the substrate amylose. Furthermore, the addition of amylomaltase (AM, EC 2.4.1.25) significantly enhanced the efficiency of this process, and the yield of ESG reached approximately 65%. Typical preparations of ESG obtained by this method were subjected to structural analyses. The average chain length, interior chain length, and exterior chain length of the ESGs were 8.2-11.6, 2.0-3.3, and 4.2-7.6, respectively. Transmission electron microscopy and intrinsic viscosity measurement showed that the ESG molecules formed spherical particles. Unlike starch, the ESGs were barely degraded by pullulanase. Solutions of ESG were opalescent (milky-white and slightly bluish), and gave a reddishbrown color on the addition of iodine. These analyses revealed that ESG shares similar molecular shapes and solution properties with natural-source glycogen. Moreover, ESG had macrophage-stimulating activity and its activity depends on the molecular weight of ESG. We successfully achieved large scale production of ESG. ESG could lead to new industrial applications, such as in the food, chemical, and pharmaceutical fields.

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“…Amylose production from cellulose is extremely interesting, not only from the viewpoint of it being an effective use of biomass, but also as a one step conversion of β 1,4 glucan to α 1,4 glucan by using multiple enzymes. 41) Conclusion and future prospects. As described in this article, we have engineered thermostable α glucan phosphorylase and established the systems to produce amylose from sucrose or cellobiose.…”

mentioning

confidence: 99%

“…We then examined another phosphorylase, cellobiose phosphorylase (EC 2.4.1.20), which catalyzes the phosphorolysis of cellobiose to produce G 1 P. 41) We have The protein samples (0.6 µg) were loaded onto a gel. After electrophoresis, the gel was stained with Coomassie Brilliant Blue.…”

mentioning

confidence: 99%