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Advances in Amylases, 2nd Edition

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: 30 June 2026 | Viewed by 1105

Special Issue Editor


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Guest Editor
Laboratory of Protein Evolution, Institute of Molecular Biology, Slovak Academy of Sciences, SK-84551 Bratislava, Slovakia
Interests: amylolytic enzymes; starch/glycogen-binding domains; glycoside hydrolases; in-silico protein structure analysis; protein bioinformatics
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Special Issue Information

Dear Colleagues,

The international symposium on the Alpha-Amylase Family (ALAMYs— http://imb.savba.sk/~janecek/Alamys/) was established in 2001. Organized once every three years, each ALAMY has been held at Smolenice Castle in Slovakia, at the Congress Centre of the Slovak Academy of Sciences. The castle is situated on a hill above the small city of Smolenice, which lies at the foot of the Small Carpathian Mountains, 60 km north-east from Bratislava. The beautiful natural surroundings and attractive interiors of the castle create a special atmosphere for scientific discussions, relaxation, and meeting friends.

This Special Issue of Molecules entitled “Advances in Amylases, 2nd Edition” aims to collect contributions presented during the 9th edition of this series of conferences, The Ninth Symposium on the Alpha-Amylase Family (ALAMY_9—http://imb.savba.sk/~janecek/Alamys/Alamy_9/), due to be held September 14–18, 2025.

This Special Issue welcomes manuscripts that explore the cloning, sequencing, expression, biochemical characterization, tertiary structure determination, structure/function relationships, and protein design and evolution of starch hydrolases and related alpha-glucan active enzymes. Topics of interest include, but are not necessarily limited to, various aspects of the main alpha-amylase enzyme clan GH-H (i.e., families GH13, GH70 and GH77), as well as of the smaller alpha-amylase families—especially GH57, but also GH119 and even GH126. Explorations of starch-active LPMOs from the family AA13 are equally welcome. Last but not least, any aspects of starch and glycogen (in general, an alpha-glucan) binding, representing distinct CBMs and/or surface-binding sites, also fall within the scope of this Special Issue. In addition to basic research-oriented studies, research exploring potential applications, especially in biotechnology and medicine, is also welcome.

Three types of contributions will be considered: (i) articles; (ii) reviews, and (iii) perspectives.

Finally, this Special Issue is open not only for participants of the ALAMY_9 Symposium; all “amylase-positive” people are welcome to contribute!

Prof. Dr. Stefan Janecek
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 250 words) can be sent to the Editorial Office for assessment.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • enzyme
  • alpha-amylase enzyme
  • starch and glycogen
  • gut microbiome oriented study

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Published Papers (1 paper)

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Research

15 pages, 2230 KB  
Article
Efficient Production of γ-CD from Starch by γ-CGTase Heterologously Produced in Pichia pastoris, Assisted by β-CGTase Liquefaction and Pullulanase Debranching
by Nuo Chen, Xiaoxiao Li, Zhengyu Jin, Birte Svensson and Yuxiang Bai
Molecules 2026, 31(4), 581; https://doi.org/10.3390/molecules31040581 - 7 Feb 2026
Viewed by 431
Abstract
Cyclodextrins (CDs) are cyclic oligosaccharides composed of α(1 → 4) linked glucose units, which are widely used as solubilizers and stabilizers in the food, pharmaceutical and cosmetic industries. Among the CDs, γ-CD has attracted much attention due to its larger hydrophobic cavity and [...] Read more.
Cyclodextrins (CDs) are cyclic oligosaccharides composed of α(1 → 4) linked glucose units, which are widely used as solubilizers and stabilizers in the food, pharmaceutical and cosmetic industries. Among the CDs, γ-CD has attracted much attention due to its larger hydrophobic cavity and higher solubility. However, the industrial production of γ-CD is limited by lack of suitable enzymes and production process shortcomings. In this study, various strategies of improving heterologous enzyme production and optimization of the starch conversion process were applied to increase the production of γ-CD. A γ-cyclodextrin glucanotransferase with good product specificity from Bacillus sp. FJAT-44876 (BFγ-CGTase) and a liquefying β-CGTase from Bacillus sp. 1011 (Bsβ-CGTase) were successfully secreted by Pichia pastoris. After codon optimization and using the one-factor-at-a-time (OFAT) principle to improve the fermentation, the yield of recombinant BFγ-CGTase was increased 13.3 times to 463 U/L. Next a process was established involving Bsβ-CGTase-assisted starch liquefaction and simultaneous pullulanase debranching and BFγ-CGTase production of γ-CD. The yield of γ-CD increased by 17.67% via optimizing the amounts of BFγ-CGTase and BtPul used for the reaction. Overall, combination of the various improvements provided a new process for efficient preparation of γ-CD. Full article
(This article belongs to the Special Issue Advances in Amylases, 2nd Edition)
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