Cloning of Isoamylase Gene of Pectobacterium carotovorum subsp. carotovorum LY34 and Identification of Essential Residues of Enzyme

Isoamylase (EC 3.2.1.68), belonging to glycoside hydrolase subfamily GH13_11, catalyzes the hydrolysis of the 𝜶-1,6-D-glucosidic linkages in amylopectin, glycogen, and derived oligosaccharides. The high debranching efficiency and transglycosylation activity enable its use in food, feed, detergent, and other industries. However, the low catalytic efficiency and insufficient stability of currently known isoamylases prevent their widespread applications. To meet the requirements set by specific applications, therefore, there is a continuing demand to obtain isoamylases with good stabilities and high expression levels by protein engineering and development of novel fermentation strategies. Herein, the microbial sources, biochemical properties, and distinct sequence and structural features of microbial isoamylases are summarized. Current developments in the protein engineering, heterologous expression, and industrial applications of isoamylases are also discussed. Finally, the future research perspectives of microbial isoamylases are provided.

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Characteristics, Protein Engineering, Heterologous Production, and Industrial Applications of Microbial Isoamylases

Dong

Yang

Dong

et al. 2021

Starch Stärke

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Analysis of two Mexican Pectobacterium brasiliense strains reveals an inverted relationship between c-di-GMP levels with exopolysaccharide production and swarming motility

Narváez-Barragán

Sandozequi

Rodríguez

et al. 2020

Microbiological Research

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The application of conventional or magnetic materials to support immobilization of amylolytic enzymes for batch and continuous operation of starch hydrolysis processes

Hermida

Agustian

2022

Reviews in Chemical Engineering

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In the production of ethanol, starches are converted into reducing sugars by liquefaction and saccharification processes, which mainly use soluble amylases. These processes are considered wasteful operations as operations to recover the enzymes are not practical economically so immobilizations of amylases to perform both processes appear to be a promising way to obtain more stable and reusable enzymes, to lower costs of enzymatic conversions, and to reduce enzymes degradation/contamination. Although many reviews on enzyme immobilizations are found, they only discuss immobilizations of α-amylase immobilizations on nanoparticles, but other amylases and support types are not well informed or poorly stated. As the knowledge of the developed supports for most amylase immobilizations being used in starch hydrolysis is important, a review describing about their preparations, characteristics, and applications is herewith presented. Based on the results, two major groups were discovered in the last 20 years, which include conventional and magnetic-based supports. Furthermore, several strategies for preparation and immobilization processes, which are more advanced than the previous generation, were also revealed. Although most of the starch hydrolysis processes were conducted in batches, opportunities to develop continuous reactors are offered. However, the continuous operations are difficult to be employed by magnetic-based amylases.

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Cloning of Isoamylase Gene of Pectobacterium carotovorum subsp. carotovorum LY34 and Identification of Essential Residues of Enzyme

Cited by 4 publications

References 21 publications

Characteristics, Protein Engineering, Heterologous Production, and Industrial Applications of Microbial Isoamylases

Characteristics, Protein Engineering, Heterologous Production, and Industrial Applications of Microbial Isoamylases

Analysis of two Mexican Pectobacterium brasiliense strains reveals an inverted relationship between c-di-GMP levels with exopolysaccharide production and swarming motility

The application of conventional or magnetic materials to support immobilization of amylolytic enzymes for batch and continuous operation of starch hydrolysis processes

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