Article
Agricultural Engineering
G. d'Ippolito, G. Squadrito, M. Tucci, N. Esercizio, A. Sardo, M. Vastano, M. Lanzilli, A. Fontana, P. Cristiani
Summary: Hyperthermophilic bioelectrochemical systems can effectively produce hydrogen and lactic acid, with dynamic polarization conditions enhancing product yields, showing potential applications for waste utilization.
BIORESOURCE TECHNOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Zuodong Sun, Bing Xu, Shaun Spisak, Jennifer M. Kavran, Steven E. Rokita
Summary: The nitroreductase superfamily contains enzymes with FMN-dependent catalysts, each with a common core and unique sequence extensions. Investigation on the outlier TnIYD from the iodotyrosine deiodinase subgroup showed that despite lacking certain standard motifs, it efficiently catalyzes dehalogenation reactions and shares similarities with IYDs from mesophiles. This study demonstrates the advantages of studying divergent sequences to uncover essential activity requirements and suggests TnIYD as a promising starting point for engineering stable dehalogenases targeting environmental halophenols.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2021)
Article
Biotechnology & Applied Microbiology
Joshua O. Ighalo, Adewale George Adeniyi, Chinenye Adaobi Igwegbe
Summary: This study investigated the morphological characteristics of T. neapolitana biofilms on various surfaces using 3D reconstruction technology, showing that carbon cloth was the most suitable electrode for the application and could better prevent bacteria detachment from the electrode surface.
BIOTECHNOLOGY LETTERS
(2021)
Article
Engineering, Chemical
Mauro Marengo, Davide Pezzilli, Eleonora Gianquinto, Alex Fissore, Simonetta Oliaro-Bosso, Barbara Sgorbini, Francesca Spyrakis, Salvatore Adinolfi
Summary: Alpha-amylases are enzymes with a wide distribution and high sequence identity, but their catalytic activities have diverged throughout evolution. By comparing alpha-amylases from human, Aspergillus oryzae, and pancreatic porcine, we found that despite structural homology, these enzymes exhibit strikingly different activities mediated by different ions. This highlights the need to carefully consider these functional differences and establish proper experimental conditions when using alpha-amylases from different organisms as models for human enzymes.
Review
Biochemistry & Molecular Biology
Beibei Wang, Daye Huang, Chunxia Cao, Yan Gong
Summary: Amylase is a crucial enzyme in insect growth and development, providing insects with strong stress resistance. Replication of the amylase gene is common in insects, allowing for changes in its location and function. The interaction between insect amylase inhibitors and amylases, as well as the effects of plant-derived inhibitors on insect and mammalian amylases, have drawn attention from researchers. Recent studies have focused on the impact of pesticides on amylase activity in both target and non-target pests, providing a theoretical basis for the development of safe and efficient pesticides. However, the exact lethal mechanisms and field application safety remain unclear. This article summarizes the latest advances in insect amylase research, including its sequence and characteristics, as well as the regulation of amylase inhibitors. Furthermore, the potential application of amylases as a nanocide trigger, RNAi, or other pesticide targets is discussed, providing a comprehensive foundation for the development of new-generation insect management tools and improving the specificity, stability, and safety of pesticides.
Article
Chemistry, Applied
Yifan Gui, Feixue Zou, Jiahao Li, Yu Zhu, Li Guo, Bo Cui
Summary: The research revealed that the activity of malt amylase was highest on the third day of incubation, significantly affecting the structure and functionality of corn starch by reducing the integrity of starch granules and increasing gelatinization temperature. The enzyme-treated starches showed an increase in pasting viscosity, providing a valuable method for preparing starch derivatives with lower cost and higher performance.
FOOD HYDROCOLLOIDS
(2021)
Review
Biotechnology & Applied Microbiology
Prayatna Sharma, Krishnendu Mondal, Keshab Chandra Mondal, Nagendra Thakur
Summary: With the development of green chemistry, the use of enzymes in industrial processes as an alternative to traditional chemical catalysts has gained significant attention. Among these enzymes, alpha-amylase stands out due to its important role in starch hydrolysis and biotechnological applications. Various methods have been devised to improve the thermostability of enzymes in response to industrial demand, including protein engineering, directed evolution, and enzyme immobilisation strategies.
WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY
(2022)
Article
Multidisciplinary Sciences
Si Jie Lim, Siti Nurbaya Oslan
Summary: This review focuses on the engineering of microbial alpha-amylases to enhance favored characteristics in industrial applications. The study demonstrates that protein engineering can improve enzyme half-life, resistance, and specificity. The results suggest that these modifications can bring significant benefits to future industrial production.
Article
Chemistry, Applied
Man Yuan, Yanli Wang, Yuxiang Bai, Birte Svensson
Summary: This study used two commercial alpha-amylases to improve the gel strength of cross-linked tapioca starch. The results showed that one alpha-amylase mainly attacked amorphous regions, while the other alpha-amylase hydrolyzed both amorphous regions and amorphous lamella of crystalline regions. The analysis of pasting and gelling properties indicated that the alpha-amylase increased the storage modulus of cross-linked starch gels, while the other alpha-amylase formed a solid gel.
FOOD HYDROCOLLOIDS
(2022)
Article
Microbiology
Dominick J. J. Jenkins, Benjamin M. M. Woolston, M. Indriati Hood-Pishchany, Paula Pelayo, Alyssa N. N. Konopaski, M. Quinn Peters, Michael T. T. France, Jacques Ravel, Caroline M. M. Mitchell, Seth Rakoff-Nahoum, Christopher Whidbey, Emily P. P. Balskus
Summary: Biochemical characterization of glycogen-degrading enzymes in vaginal bacteria reveals their role in metabolizing glycogen and shaping the vaginal microbiota.
NATURE MICROBIOLOGY
(2023)
Review
Biochemistry & Molecular Biology
Aleksandr P. Kalinovskii, Oksana V. Sintsova, Irina N. Gladkikh, Elena V. Leychenko
Summary: This review focuses on the structural diversity and action mechanisms of active natural products with inhibitory activity toward mammalian alpha-amylases, and emphasizes proteinaceous inhibitors as more effective compounds with significant potential for clinical use.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Susu Yuan, Renxiang Yan, Biyu Lin, Renkuan Li, Xiuyun Ye
Summary: This study successfully improved the thermostability of medium-temperature alpha-amylase by altering certain amino acids in BAA. The analysis of predicted structures revealed that the mutant had more calcium-binding sites and intramolecular interactions, as well as reduced steric hindrance at the active cavity, which contributed to the increased thermostability. These findings provide reference values for the modification of alpha-amylases.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2023)
Article
Microbiology
Matheus Mertz Ribeiro, Maria Ines Rezende, Cristiani Baldo, Daniele Sartori
Summary: Aspergillus welwitschiae strains show great potential in producing amylases for biotechnological applications, with high catalytic efficiency at different pH and temperature.
CURRENT MICROBIOLOGY
(2022)
Article
Biochemistry & Molecular Biology
Zuzana Janickova, Stefan Janecek
Summary: This study conducted a detailed bioinformatics analysis on fungal and chloride-dependent alpha-amylases from the GH13 family, identifying conserved sequence regions and focusing on the GH13_32 subfamily. Evolutionary relationships between these enzymes were demonstrated through two evolutionary trees based on sequence alignments.
Article
Biology
Havva Esra Tutuncu, Yusuf Surmeli
Summary: This study conducted a comparative analysis of three thermoalkaliphilic GH13 alpha-amylases from different bacterial sources, focusing on their evolutionary relationships, enzyme sequence similarities, three-dimensional structures, and protein-ligand interactions. The results showed that these alpha-amylases exhibited differences in structure and function, and they could be potential candidates for industrial processes that require thermoalkaliphilic properties.