Amylase

ISSN: 2450-9728

Edited by: Stefan Janecek

About this journal

Amylase was an international, peer-reviewed, open-access journal that published top-quality original research, insightful reviews and hot news in the field of amylolytic and related enzymes in its widest sense. General scope was any work focused on cloning and sequencing, expression and biochemical characterization, tertiary structure determination, structure/function relationships and protein design as well as the evolution of starch hydrolases and related alpha-glucan active enzymes with the emphasis on their application in biotechnology and medicine.

The journal is closed for submissions.

The journal was published in Open Access model and is archived in Portico.

All authors retain copyright, unless – due to their local circumstances – their work is not copyrighted. The copyrights are governed by the Creative-Commons license.

Why read

Publication of outstanding original research papers and critical review articles in the field of amylolytic and related enzymes from all over the world.

The journal was edited by:
Journal Editor:
Stefan Janecek, Slovak Academy of Sciences & University of SS Cyril and Methodius, Skopje, Slovakia

Abstracting and Indexing

Amylase is covered by the following services:

Baidu Scholar
Cabells Journalytics
Chronos Hub
CNKI Scholar (China National Knowledge Infrastructure)
CNPIEC - cnpLINKer
Dimensions
EBSCO Discovery Service
Google Scholar
J-Gate
JournalTOCs
KESLI-NDSL (Korean National Discovery for Science Leaders)
MyScienceWork
Naver Academic
Naviga (Softweco)
Primo Central (ExLibris)
ProQuest (relevant databases)
Publons
QOAM (Quality Open Access Market)
ReadCube
Scilit
Semantic Scholar
Sherpa/RoMEO
Summon (ProQuest)
TDNet
Ulrich's Periodicals Directory/ulrichsweb
WanFang Data
WorldCat (OCLC)
X-MOL
Yewno Discover

Supplementary Materials

Topics

External Links

Volume 6 Issue 1

January 2022

Open Access January 17, 2022

How many α-amylase GH families are there in the CAZy database?

Štefan Janeček, Birte Svensson

Page range: 1-10

More Download PDF

Abstract

The CAZy database is a web-server for sequence-based classification of carbohydrate-active enzymes that has become the worldwide and indispensable tool for scientists engaged in this research field. It was originally created in 1991 as a classification of glycoside hydrolases (GH) and currently, this section of CAZy represents its largest part counting 172 GH families. The present Opinion paper is devoted to the specificity of α-amylase (EC 3.2.1.1) and its occurrence in the CAZy database. Among the 172 defined GH families, four, i.e. GH13, GH57, GH119 and GH126, may be considered as the α-amylase GH families. This view reflects a historical background and traditions widely accepted during the previous decades with respect to the chronology of creating the individual GH families. It obeys the phenomenon that some amylolytic enzymes, which were used to create the individual GH families and were originally known as α-amylases, according to current knowledge from later, more detailed characterization, need not necessarily represent genuine α-amylases. Our Opinion paper was therefore written in an effort to invite the scientific community to think about that with a mind open to changes and to consider the seemingly unambiguous question in the title as one that may not have a simple answer.

Open Access March 7, 2022

The role of the C domain in the thermostability of GH70 enzymes investigated by domain swapping

Manon Molina, Thomas Prévitali, Claire Moulis, Gianluca Cioci, Magali Remaud-Siméon

Page range: 11-19

More Download PDF

Abstract

Sucrose-active enzymes belonging to the glycoside hydrolase (GH) family 70 are attractive tools for the synthesis of oligosaccharides, polysaccharides or glycoconjugates. However, their thermostability is an important issue for the development of robust and cost-effective enzyme-based processes. Indeed, GH70 enzymes are mesophilic and no thermophilic representatives have been described so far. Furthermore, structurally guided engineering is a challenge given the size of these proteins (120 to 250 kDa) and their organization in five domains. Herein, we have investigated the possible role of the domain C in the stability of GH70 enzymes. The alternansucrase (ASR) is the most stable enzyme of the GH70 family. Structural comparison of ASR to other GH70 enzymes highlighted the compactness of its domain C. We assumed that this atypical structure might be involved in the stability of this enzyme and decided to introduce this domain in another much less stable GH70 enzyme of known three-dimensional structure, the branching sucrase GBD-CD2. The chimeric GBD-CD2 exhibited a lower specific activity on sucrose substrate but its specificity was unchanged with the enzyme remaining specific for the branching of dextran via α-1,2 linkage formation. Interestingly, the chimera showed a higher melting temperature and residual activity than the wild-type enzyme after 10 min incubation at 30 °C showing that the domain C can affect GH70 enzyme stability and could be a potential target of both random or rational mutagenesis to further improve their stability.

No ranking information is available for this journal.

Editorial

Managing Editor
Izabela Zarczynska
izabela.zarczynska@degruyter.com

(Deutsch)

Type: Journal
Language: English
Publisher: De Gruyter Open Access
First published: January 1, 2016
Last published: January 1, 2022
Publication Frequency: 1 Issue per Year
Audience: Students and researchers at various stages of academic career, specializing in plant biology, physiology, insect physiology, entomology, agriculture, biochemistry