Immobilization of Polysaccharide-degrading Enzymes

Storey, Kenneth B.; Schafhauser-Smith, Doris Y.

doi:10.1080/02648725.1994.10647918

Cited by 11 publications

(2 citation statements)

References 84 publications

(230 reference statements)

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“…The amount of CmBAM remaining in the supernatant after immobilization was 62–71% of the amount of protein added, indicating that CmBAM activity remained active after immobilization (Figure B). The activity of the immobilized enzyme may be reduced by the physical constraints of the polymer, such as starch . In addition, since the amino acid residues that bind to the carrier are random, there is a risk of inhibition of the active site.…”

Section: Discussionmentioning

confidence: 99%

“…The activity of the immobilized enzyme may be reduced by the physical constraints of the polymer, such as starch. 43 In addition, since the amino acid residues that bind to the carrier are random, there is a risk of inhibition of the active site. However, the immobilization of CmBAM on silica gel carriers did not suffer from the inhibition described above.…”

Section: Discussionmentioning

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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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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

Murakami

Osanai

2022

ACS Omega

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Bioorganic Catalysts and Catalysis

Pannuri

DiSanto

Kamat

2002

Encyclopedia of Catalysis

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Bioorganic catalysis is emerging as a powerful tool to complement traditional catalytic reactions in organic synthesis. A wide range of reactions can be catalyzed using biocatalysts, and this article attempts to introduce the reader to the variety of reactions that have been demonstrated. Although these reactions are possible in the laboratory, the challenge is to make them economically feasible on an industrial scale. Each biotransformation process has some unique obstacles to overcome before it is translated from the laboratory to commercial scale, and some of these problems are discussed. Biocatalytic properties are amenable to dramatic modification using genetic and solvent engineering, setting them apart from traditional catalysts. Many biocatalytic processes are being run on a commercial scale and one such reaction utilizing a transaminase is presented as a case study.

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