Reversible Glucan Phosphorylation in the Red Alga, Cyanidioschyzon merolae

Brizzee, Corey O.

doi:10.13023/etd.2021.216

Cited by 1 publication

(3 citation statements)

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“…2.4.1.25, disproportionating enzymes, DPE1 or 2) and isoamylase, and C. merolae has minimal enzymes compared to higher plants and green algae . In the starch hydrolysis pathway of C.…”

Section: Introductionmentioning

confidence: 99%

“…merolae, two isoamylases and one pullulanase cleave the α-1,6 glycosidic linkages of glucans, whereas only one β-amylase hydrolyzes α-1,4 glycosidic linkages. These enzymes cannot directly cleave granular starch, but they phosphorylate and solubilize the surface of starch granules through glucan-water dikinase (GWD), leading to cleaving by various carbohydrate-hydrolyzing enzymes . Maltose produced by the coupling of isoamylase, pullulanase, and β-amylase is metabolized by 4-α-glucanotransferase (DPE2). , β-Amylases are widely distributed among both prokaryote and eukaryote, and the catalytic domain, consisting of two glutamate residues and a flexible loop, is identified .…”

Section: Introductionmentioning

confidence: 99%

“…2.4.1.25, disproportionating enzymes, DPE1 or 2) and isoamylase, and C. merolae has minimal enzymes compared to higher plants and green algae. 28 In the starch hydrolysis pathway of C. merolae , two isoamylases and one pullulanase cleave the α-1,6 glycosidic linkages of glucans, whereas only one β-amylase hydrolyzes α-1,4 glycosidic linkages. These enzymes cannot directly cleave granular starch, but they phosphorylate and solubilize the surface of starch granules through glucan-water dikinase (GWD), leading to cleaving by various carbohydrate-hydrolyzing enzymes.…”

Section: Introductionmentioning

confidence: 99%

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Biochemical Properties of β-Amylase from Red Algae and Improvement of Its Thermostability through Immobilization

Murakami

Osanai

2022

ACS Omega

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β-Amylase hydrolyzes polysaccharides, such as starch, into maltose. It is used as an industrial enzyme in the production of food and pharmaceuticals. The eukaryotic red alga Cyanidioschyzon merolae is a unicellular alga that grows at an optimum pH of 2.0−3.0 and an optimum temperature of 40−50 °C. By focusing on the thermostability and acid resistance of the proteins of C. merolae, we investigated the properties of β-amylase from C. merolae (hereafter CmBAM) and explored the possibility of using CmBAM as an industrial enzyme. CmBAM showed the highest activity at 47 °C and pH 6.0. CmBAM had a relatively higher specificity for amylose as a substrate than for starch. Immobilization of CmBAM on a silica gel carrier improved storage stability and thermostability, allowing the enzyme to be reused. The optimum temperature and pH of CmBAM were comparable to those of existing β-amylases from barley and wheat. C. merolae does not use amylose, but CmBAM has a substrate specificity for both amylose and amylopectin but not for glycogen. Among the several β-amylases reported, CmBAM was unique, with a higher specificity for amylose than for starch. The high specificity of CmBAM for amylose suggests that isoamylase and pullulanase, which cleave the α-1,6 bonds of starch, may act together in vivo. Compared with several reported immobilized plant-derived β-amylases, immobilized CmBAM was comparable to β-amylase, with the highest reusability and the third-highest storage stability at 30 days of storage. In addition, immobilized CmBAM has improved thermostability by 15−20 °C, which can lead to wider applications and easier handling.

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“…2.4.1.25, disproportionating enzymes, DPE1 or 2) and isoamylase, and C. merolae has minimal enzymes compared to higher plants and green algae . In the starch hydrolysis pathway of C.…”

Section: Introductionmentioning

confidence: 99%