Properties and applications of starch-converting enzymes of the α-amylase family

  title={Properties and applications of starch-converting enzymes of the $\alpha$-amylase family},
  author={Marc van der Maarel and Bart A. van der Veen and Joost C. M. Uitdehaag and Hans Leemhuis and Lubbert Dijkhuizen},
  journal={Journal of Biotechnology},

Figures and Tables from this paper

Starch-processing enzymes – emphasis on thermostable 4-α-glucanotransferases

Abstract Starch is a major storage product of several economically important crops and the most common carbohydrate in human diets. A variety of enzymes are capable of starch hydrolysis and a

Application of microbial α-amylase in industry - A review

This review focuses on the production of bacterial and fungal α-amylases, their distribution, structural-functional aspects, physical and chemical parameters, and the use of these enzymes in industrial applications.

Properties and applications of starch modifying enzymes for use in the baking industry

These developments of enzyme technology highlight the potential to create various structured-starches for the food and baking industry.

Starch-Modifying Enzymes.

    S. Hashim
    Advances in biochemical engineering/biotechnology
  • 2019
Alkaline-active amylases are applicable in the paper, textile and leather industries and also in bioremediation and alkaline waste water treatment, and their application in these fields is further enhanced through stabilization and improving their specificity and catalytic action by employing nanotechnology and genetic engineering.

α-Amylases from Microbial Sources and Its Potential Applications in Various Industries

The production of α-amylase is essential for conversion of starches into oligosaccharides, and the properties of each α-Amylase such as thermostability, pH profile, pH stability, and Ca-independency are important in the development of fermentation process.

α-Amylases from Microbial Sources and Its Potential Applications in Various Industries

Amylases are widely distributed and are one of the most studied enzymes. Such enzymes hydrolyze the starch molecules into polymers composed of glucose units. Amylases have potential application in a

Microbial Starch-Converting Enzymes: Recent Insights and Perspectives.

This review provides current information on enzymes belonging to GH13, 57, 70, and 77 that can be used in structural modifications of the starch polysaccharides or to produce starch-derived products from them.

Unique features of several microbial α-amylases active on soluble and native starch

Results demonstrate that starch granules are inert and require specialized amylase enzymes to be completely degraded, which could be used in a non-cooking starch conversion process, reducing the amount of energy required in the production of glucose syrups for bioethanol fermentation.

Protein engineering of amylases.

It may be possible, therefore, to design amylolytic enzymes with altered properties on the basis of sequence comparison using known properties of functional side-chains, the tertiary structure of a related enzyme, and the predicted secondary structure.

Enzymes involved in the processing of starch to sugars

Advances in microbial amylases.

The molecular biology of amylases is discussed, describing structures, cloning, sequences, and protoplast fusion and mutagenesis, followed by sections on their production and finally the properties of various amylase.

Production of Cyclodextrins, a Novel Carbohydrate, in the Tubers of Transgenic Potato Plants

This work attempted to engineer the tubers of developing potatoes to produce these novel, high–value carbohydrates using a CGT gene from Klebsiella, and produced α, β, and β CDs.

Protein engineering of bacterial α-amylases

Potato D-enzyme Catalyzes the Cyclization of Amylose to Produce Cycloamylose, a Novel Cyclic Glucan (*)

Analysis of the products indicated that the enzyme catalyzes an intramolecular transglycosylation reaction on amylose to produce cyclic α-1,4-glucan (cycloamylose), and confirmation of the cyclic structure was achieved by demonstrating the absence of reducing and nonreducing ends, resistance to hydrolysis by glucoamylase, and by “time of flight” mass spectrometry.

Molecular and industrial aspects of glucose isomerase.

Manipulation of the GI gene by site-directed mutagenesis holds promise that a GI suitable for biotechnological applications will be produced in the foreseeable future.

Commodity scale production of sugars from starches.

Enzymatic Characterisation of Novamyl®, a Thermostable α‐Amylase

The new data presented here clearly show that unlike exoamylases, Novamyl® does not require a non-reducing end and attacks amylose, Indp5 and cyclodextrins in an endo-like manner.

Cyclization reaction catalyzed by branching enzyme

The action of branching enzyme from Bacillus stearothermophilus on amylose was analyzed and it was suggested that branching enzyme catalyzed cyclization of the alpha-l,4-glucan chain of theAmylose molecule to form an alpha- l,6-glUCosidic linkage, thereby forming two smaller molecules.