Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
10.3
5.1
Journals
Molecules
Special Issues
Advances in Amylases, 2nd Edition
molecules-logo
Submit to Special Issue Submit Abstract to Special Issue Review for Molecules Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

Advances in Amylases, 2nd Edition

A Special Issue of Molecules (ISSN 1420-3049) belonging to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: 30 November 2026 | Viewed by 3426

Editor

Prof. Dr. Stefan Janecek

E-Mail Website
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
Special Issues, Collections and Topics in MDPI journals

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-anonymized 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

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

Further information on MDPI's Special Issue policies can be found here.

Related Special Issue

Published Papers (4 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Other

23 pages, 10566 KB  
Article
Structure and Function of Honeybee α-Amylase of Glycoside Hydrolase Family 13 Subfamily 15
by Wataru Saburi, Yushi Takahashi, Shiho Takei, Toyoyuki Ose and Haruhide Mori
Molecules 2026, 31(15), 2615; https://doi.org/10.3390/molecules31152615 - 27 Jul 2026
Viewed by 529
Abstract
α-Amylase, ubiquitously distributed across diverse organisms, catalyzes the hydrolysis of the internal α-(1→4)-linkage of α-(1→4)-glucan including starch as an essential energy source. Insect α-amylases, which belong to the glycoside hydrolase family 13 subfamily 15 (GH13_15), are important for optimal larval growth and adult [...] Read more.
α-Amylase, ubiquitously distributed across diverse organisms, catalyzes the hydrolysis of the internal α-(1→4)-linkage of α-(1→4)-glucan including starch as an essential energy source. Insect α-amylases, which belong to the glycoside hydrolase family 13 subfamily 15 (GH13_15), are important for optimal larval growth and adult longevity. Honeybee (Apis mellifera) α-amylase (AMA) is expressed in the hypopharyngeal glands of forager bees and secreted into honey. AMA in honey, which is important for food quality control, has been partly characterized. However, its structure–function relationship is poorly understood. Herein, we present biochemical, structural, and mutational analyses of AMA. Kinetic analysis using p-nitrophenyl maltooligosaccharides and their 4,6-benzylidene-modified derivatives revealed a subsite affinity map of AMA. AMA contains high-affinity subsites −3, −2, +1, and +2, similar to those of the mammalian α-amylases of GH13_24. Most AMA substrate-binding residues are conserved in the GH13_24 enzymes. Mutational analysis revealed that Leu175 is crucial at subsites −3/−2 for reactions with oligo- and polysaccharides. Furthermore, Trp77 at subsites −3/−2 and Lys210 at subsite +2 are suggested to be involved in the proper binding of long-chain substrates. AMA shares a surface sugar-binding site with mammalian α-amylases, where Asn281, Trp285, and Trp293 are essential for the binding and degradation of starch granules. Full article
(This article belongs to the Special Issue Advances in Amylases, 2nd Edition)
►▼ Show Figures

Graphical abstract

19 pages, 7043 KB  
Article
In Silico Study of Potential Binding Sites of the Family GH126 Enzyme CPF_2247 from Clostridium perfringens Using Structural Comparison and Molecular Docking Methods
by Michaela Hodorová and Štefan Janeček
Molecules 2026, 31(13), 2273; https://doi.org/10.3390/molecules31132273 - 29 Jun 2026
Viewed by 477
Abstract
The family GH126 represents a potential fourth, but still non-confirmed α-amylase family in CAZy with the founding, partially characterized member, the assumed amylolytic enzyme CPF_2247 from Clostridium perfringens. Proteins of this family adopt an (α/α)6-barrel domain, structurally distinct from the [...] Read more.
The family GH126 represents a potential fourth, but still non-confirmed α-amylase family in CAZy with the founding, partially characterized member, the assumed amylolytic enzyme CPF_2247 from Clostridium perfringens. Proteins of this family adopt an (α/α)6-barrel domain, structurally distinct from the rather more complex domain arrangement of families GH13, GH57, and GH119. Interestingly, GH126 exhibits structural similarity, including sharing potential functionally important residues with inverting β-glucanases from GH8 and GH48 (clan GH-M); this fact has prompted previous bioinformatics analyses. In the present study, two GH126 members with experimentally determined tertiary structure—the CPF_2247 and the exopolysaccharide-specific hydrolase PssZ from Listeria monocytogenes—were compared with seven GH8 and ten GH48 enzyme-substrate complexes. Family GH126 enzymes display a wide, open binding cleft, with a central tunnel-like cavity along the barrel axis, distinct from the narrow cleft in GH8 and the tunnel-shaped site in GH48. Conserved residues involved in substrate binding and catalysis of GH8 and GH48 were identified in GH126. Molecular docking with α-glucans using the CPF_2247 confirmed predicted binding at the potential active site and revealed also eventual additional binding sites. Targeted docking showed the strongest interactions for acarbose and maltoheptaose, particularly involving a GH126 unique α11-α12 loop in the assumed amylolytic enzyme CPF_2247. Full article
(This article belongs to the Special Issue Advances in Amylases, 2nd Edition)
►▼ Show Figures

Figure 1

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 872
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)
►▼ Show Figures

Figure 1

Other

Jump to: Research

20 pages, 2612 KB  
Perspective
Beyond Branching: Unlocking the Catalytic Versatility of Branching Enzymes for the Design of Diverse α-Glucan Structures
by Maurice K. H. Essers, Hans Leemhuis, Johannes H. Bitter and Lambertus A. M. van den Broek
Molecules 2026, 31(16), 2821; https://doi.org/10.3390/molecules31162821 - 13 Aug 2026
Viewed by 464
Abstract
Starch-modifying glycoside hydrolases (GHs) typically operate via a retaining double-displacement mechanism, involving formation of a covalent glycosyl–enzyme intermediate. This intermediate can be resolved either by water, resulting in hydrolysis, or by a glucan acceptor, leading to transglucosylation. Many GHs exhibit both catalytic activities, [...] Read more.
Starch-modifying glycoside hydrolases (GHs) typically operate via a retaining double-displacement mechanism, involving formation of a covalent glycosyl–enzyme intermediate. This intermediate can be resolved either by water, resulting in hydrolysis, or by a glucan acceptor, leading to transglucosylation. Many GHs exhibit both catalytic activities, although they are classified according to their predominant reaction. For example, branching enzymes (BEs) catalyse α-(1→4) bond cleavage and α-(1→6) branch formation via transglucosylation, while also exhibiting minor hydrolytic and disproportionation activities that broaden their catalytic repertoire. More recent research indicates that the different catalytic activities of BEs can be interconnected, thereby collectively determining the final α-glucan architecture. This challenges the classical view that the predominant branching activity of BEs is catalysed independently. Moreover, the balance between these coupled activities influences substrate specificity and can broaden the substrate scope to include chemically modified starches. Furthermore, the co-application of BEs with other GHs reveals synergistic interactions between catalytic activities, enabling the generation of α-glucan structures that cannot be produced by any of the enzymes individually. In this perspective paper, and based on recent developments, we argue that the catalytic framework of BEs provides multiple strategies for tailoring diverse α-glucan architectures. This enables modulation of structural features across hierarchical levels, from supramolecular to macromolecular organisation. As a result, BEs represent versatile tools for engineering starch functionality beyond digestibility, extending their potential toward pharmaceutical and non-food applications. Looking ahead, we discuss how enzyme-designed and chemically functionalised α-glucan polymers may emerge as a new class of sustainable materials. These materials could provide biodegradable, water-soluble, and renewable alternatives to petrochemical-derived polymers used in personal and home care products. Full article
(This article belongs to the Special Issue Advances in Amylases, 2nd Edition)
►▼ Show Figures

Graphical abstract

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-4
Back to TopTop