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BioMed Research International 2017Amylase is an important and indispensable enzyme that plays a pivotal role in the field of biotechnology. It is produced mainly from microbial sources and is used in... (Review)
Review
Amylase is an important and indispensable enzyme that plays a pivotal role in the field of biotechnology. It is produced mainly from microbial sources and is used in many industries. Industrial sectors with top-down and bottom-up approaches are currently focusing on improving microbial amylase production levels by implementing bioengineering technologies. The further support of energy consumption studies, such as those on thermodynamics, pinch technology, and environment-friendly technologies, has hastened the large-scale production of the enzyme. Herein, the importance of microbial (bacteria and fungi) amylase is discussed along with its production methods from the laboratory to industrial scales.
Topics: Amylases; Bacteria; Biotechnology; Fungi; Industry; Substrate Specificity
PubMed: 28280725
DOI: 10.1155/2017/1272193 -
The Journal of Clinical Pediatric... Nov 2021The aim of the study was to assess the salivary IgA (immunoglobulin A) and alpha amylase levels in the unstimulated whole saliva samples of caries-free and caries-active... (Comparative Study)
Comparative Study
OBJECTIVES
The aim of the study was to assess the salivary IgA (immunoglobulin A) and alpha amylase levels in the unstimulated whole saliva samples of caries-free and caries-active children and correlate it with the caries status and age.
STUDY DESIGN
The salivary IgA and amylase was investigated in 100 children in the range of 8-12 years divided in two groups, control group (DMFT and/or deft = 0) and study group (DMFT/deft score ≥5). The salivary IgA was measured using kit based on two-site sandwich enzyme immunoassay principle and amylase was estimated using the vitro amyl slides.
RESULTS
The mean salivary IgA and amylase levels in the saliva of the children in the control group was found to be significantly increased (p=.001 and p=.014 respectively) whereas the relationship between salivary IgA and amylase levels in the saliva of the children was found to be insignificant with the age (p=.392 and p=.306 respectively).
CONCLUSIONS
The results indicated that salivary IgA and amylase levels in saliva increased significantly in caries free children and the level of salivary IgA and alpha amylase has no significant relation with the age of the children.
Topics: Amylases; Child; Dental Caries; Dental Caries Susceptibility; Humans; Immunoglobulin A; Saliva; alpha-Amylases
PubMed: 34740270
DOI: 10.17796/1053-4625-45.5.6 -
Molecules (Basel, Switzerland) Jan 2019Momilactones A (MA) and B (MB) are the active phytoalexins and allelochemicals in rice. In this study, MA and MB were purified from rice husk of cv. Koshihikari by...
Momilactones A (MA) and B (MB) are the active phytoalexins and allelochemicals in rice. In this study, MA and MB were purified from rice husk of cv. Koshihikari by column chromatography, and purification was confirmed by high-performance liquid chromatography, thin-layer chromatography, gas chromatography-mass spectrometry, liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS), and ¹H and C nuclear magnetic resonance analyses. By in vitro assays, both MA and MB exerted potent inhibition on α-amylase and α-glucosidase activities. The inhibitory effect of MB on these two key enzymes was greater than that of MA. Both MA and MB exerted greater α-glucosidase suppression as compared to that of the commercial diabetic inhibitor acarbose. Quantities of MA and MB in rice grain were 2.07 ± 0.01 and 1.06 ± 0.01 µg/dry weight (DW), respectively. This study was the first to confirm the presence of MA and MB in refined rice grain and reported the α-amylase and α-glucosidase inhibitory activity of the two compounds. The improved protocol of LC-ESI-MS in this research was simple and effective to detect and isolate MA and MB in rice organs.
Topics: Amylases; Diterpenes; Glycoside Hydrolase Inhibitors; Lactones; Oryza; alpha-Amylases; alpha-Glucosidases
PubMed: 30700006
DOI: 10.3390/molecules24030482 -
BMC Genomics Apr 2023Starch hydrolysates are energy sources for plant growth and development, regulate osmotic pressure and transmit signals in response to both biological and abiotic...
BACKGROUND
Starch hydrolysates are energy sources for plant growth and development, regulate osmotic pressure and transmit signals in response to both biological and abiotic stresses. The α-amylase (AMY) and the β-amylase (BAM) are important enzymes that catalyze the hydrolysis of plant starch. Cassava (Manihot esculenta Crantz) is treated as one of the most drought-tolerant crops. However, the mechanisms of how AMY and BAM respond to drought in cassava are still unknown.
RESULTS
Six MeAMY genes and ten MeBAM genes were identified and characterized in the cassava genome. Both MeAMY and MeBAM gene families contain four genes with alternative splicing. Tandem and fragment replications play important roles in the amplification of MeAMY and MeBAM genes. Both MeBAM5 and MeBAM10 have a BZR1/BES1 domain at the N-terminus, which may have transcription factor functions. The promoter regions of MeAMY and MeBAM genes contain a large number of cis-acting elements related to abiotic stress. MeAMY1, MeAMY2, MeAMY5, and MeBAM3 are proven as critical genes in response to drought stress according to their expression patterns under drought. The starch content, soluble sugar content, and amylase activity were significantly altered in cassava under different levels of drought stress.
CONCLUSIONS
These results provide fundamental knowledge for not only further exploring the starch metabolism functions of cassava under drought stress but also offering new perspectives for understanding the mechanism of how cassava survives and develops under drought.
Topics: Drought Resistance; Manihot; beta-Amylase; alpha-Amylases; Droughts; Gene Expression Regulation, Plant; Stress, Physiological; Plant Proteins
PubMed: 37024797
DOI: 10.1186/s12864-023-09282-9 -
Molecules (Basel, Switzerland) Dec 2023Amylase is an indispensable hydrolase in insect growth and development. Its varied enzymatic parameters cause insects to have strong stress resistance. Amylase gene... (Review)
Review
Amylase is an indispensable hydrolase in insect growth and development. Its varied enzymatic parameters cause insects to have strong stress resistance. Amylase gene replication is a very common phenomenon in insects, and different copies of amylase genes enable changes in its location and function. In addition, the classification, structure, and interaction between insect amylase inhibitors and amylases have also invoked the attention of researchers. Some plant-derived amylase inhibitors have inhibitory activities against insect amylases and even mammalian amylases. In recent years, an increasing number of studies have clarified the effects of pesticides on the amylase activity of target and non-target pests, which provides a theoretical basis for exploring safe and efficient pesticides, while the exact lethal mechanisms and safety in field applications remain unclear. Here, we summarize the most recent advances in insect amylase studies, including its sequence and characteristics and the regulation of amylase inhibitors (α-AIs). Importantly, the application of amylases as the nanocide trigger, RNAi, or other kinds of pesticide targets will be discussed. A comprehensive foundation will be provided for applying insect amylases to the development of new-generation insect management tools and improving the specificity, stability, and safety of pesticides.
Topics: Animals; alpha-Amylases; Amylases; Enzyme Inhibitors; Insecta; Pest Control; Pesticides
PubMed: 38067617
DOI: 10.3390/molecules28237888 -
BMC Microbiology Aug 2022Bacteria usually secrete a variety of extracellular enzymes to degrade extracellular macromolecules to meet their nutritional needs and enhance their environmental...
BACKGROUND
Bacteria usually secrete a variety of extracellular enzymes to degrade extracellular macromolecules to meet their nutritional needs and enhance their environmental adaptability. Bacillus cereus 0-9, a biocontrol bacterial strain isolated from wheat roots, has three genes annotated as encoding amylases in the genome, but their functions are unknown, and whether they are involved in the colonization process of the bacterium remains to be further studied.
METHODS
Mutant gene strains and fluorescently tagged strains were constructed by homologous recombination, and amylase protein was expressed in the prokaryotic Escherichia coli BL21(DE3) expression system. The iodine staining method was used to measure the activity of amylase proteins. We further observed the colonization abilities of the test strains in wheat roots through frozen section technology.
RESULTS
The results showed that there were three amylase-encoding genes, amyC, amyP and amyS, in the B. cereus 0-9 genome. Among the three amylase encoding genes, only amyS produced extracellular amylase whose secretion was related to signal peptide at position 1-27. The AmyS protein encoded by the amyS gene is an α-amylase. The growth of Rhizoctonia cerealis was inhibited 84.7% by B. cereus 0-9, but the biocontrol ability of the ΔamyS strain decreased to 43.8% and that of ΔamyS/amyS was restored when the amyS gene was complemented. Furthermore, the biocontrol ability of the ΔamySec strain was decreased to 46.8%, almost the same as that of the ΔamyS mutant. Due to the deletion of the amyS gene, the colonization capacities of ΔamyS (RFP) and ΔamySec (RFP) in wheat roots decreased, while that of ΔamyS/amyS (RFP) was restored after the amyS gene was complemented, indicating that the amyS gene influences the colonization of B. cereus 0-9 in wheat roots. In addition, the colonization and biocontrol abilities of the mutant were restored after the addition of sugars, such as glucose and maltose.
CONCLUSIONS
B. cereus 0-9 encodes three genes annotated as amylases, amyC, amyP and amyS. Only the deletion of the amyS gene with a signal peptide did not produce extracellular amylase. The AmyS protein encoded by the amyS gene is an α-amylase. Our results indicated that the amyS gene is closely related to the colonization abilities of B. cereus 0-9 in wheat roots and the biocontrol abilities of B. cereus 0-9 to fight against R. cerealis. The extracellular amylase produced by B. cereus 0-9 can hydrolyze starch and use glucose, maltose and other nutrients to meet the needs of bacterial growth. Therefore, it is very possible that the secretion and hydrolytic activities of extracellular amylase can promote the colonization of B. cereus 0-9 in wheat roots and play important roles in the prevention and control of plant diseases. Our results contribute to exploring the mechanisms of microbial colonization in plant roots.
Topics: Amylases; Bacillus cereus; Bacterial Proteins; Escherichia coli; Glucose; Maltose; Plant Roots; Protein Sorting Signals; Triticum; alpha-Amylases
PubMed: 35996113
DOI: 10.1186/s12866-022-02618-7 -
Food Research International (Ottawa,... Jul 2022The relation between contamination by trichothecenes, DON (Deoxyvalenol) and 15-ADON (15-acetil-deoxyvalenol), and enzymes, protease, β-amylase and α-amylase, in the...
The relation between contamination by trichothecenes, DON (Deoxyvalenol) and 15-ADON (15-acetil-deoxyvalenol), and enzymes, protease, β-amylase and α-amylase, in the mashing step was studied. Malted barley was subject to mashing at three temperature ramps, which resulted in enzyme extracts. Enzyme activity of the extract was evaluated in a model solution with DON and 15-ADON. Results indicated that activities of protease and β-amylase are changed by trichothecenes. Reduction in 15-ADON concentration was 100% when the initial concentration was 0.23 µg mL and 74, 72 and 92% when it was 0.85 µg mL, under activities of protease, β-amylase and α-amylase, respectively. On the other hand, DON concentration increased 45 and 30% under protease and β-amylase activities, respectively. Malt contamination by DON and 15-ADON can affect enzyme activity and modify the process yield, which may cause economic losses.
Topics: Mycotoxins; Peptide Hydrolases; Trichothecenes; alpha-Amylases; beta-Amylase
PubMed: 35761607
DOI: 10.1016/j.foodres.2022.111317 -
International Journal of Molecular... Jan 2019Alpha-amylase, the major form of amylase with secondary carbohydrate binding sites, is a crucial enzyme throughout the growth period and life cycle of angiosperm. In... (Review)
Review
Alpha-amylase, the major form of amylase with secondary carbohydrate binding sites, is a crucial enzyme throughout the growth period and life cycle of angiosperm. In rice, alpha-amylase isozymes are critical for the formation of the storage starch granule during seed maturation and motivate the stored starch to nourish the developing seedling during seed germination which will directly affect the plant growth and field yield. Alpha-amylase has not yet been studied intensely to understand its classification, structure, expression trait, and expression regulation in rice and other crops. Among the 10-rice alpha-amylases, most were exclusively expressed in the developing seed embryo and induced in the seed germination process. During rice seed germination, the expression of alpha-amylase genes is known to be regulated negatively by sugar in embryos, however positively by gibberellin (GA) in endosperm through competitively binding to the specific promoter domain; besides, it is also controlled by a series of other abiotic or biotic factors, such as salinity. In this review, we overviewed the research progress of alpha-amylase with focus on seed germination and reflected on how in-depth work might elucidate its regulation and facilitate crop breeding as an efficient biomarker.
Topics: Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Plant; Germination; Multigene Family; Oryza; Phenotype; Plant Development; Quantitative Trait, Heritable; Seeds; Structure-Activity Relationship; alpha-Amylases
PubMed: 30669630
DOI: 10.3390/ijms20020450 -
BMC Microbiology Feb 2016Amylases and cellulases have great potential for application in industries such as food, detergent, laundry, textile, baking and biofuels. A common requirement in these...
BACKGROUND
Amylases and cellulases have great potential for application in industries such as food, detergent, laundry, textile, baking and biofuels. A common requirement in these fields is to reduce the temperatures of the processes, leading to a continuous search for microorganisms that secrete cold-active amylases and cellulases. Psychrotolerant yeasts are good candidates because they inhabit cold-environments. In this work, we analyzed the ability of yeasts isolated from the Antarctic region to grow on starch or carboxymethylcellulose, and their potential extracellular amylases and cellulases.
RESULT
All tested yeasts were able to grow with soluble starch or carboxymethylcellulose as the sole carbon source; however, not all of them produced ethanol by fermentation of these carbon sources. For the majority of the yeast species, the extracellular amylase or cellulase activity was higher when cultured in medium supplemented with glucose rather than with soluble starch or carboxymethylcellulose. Additionally, higher amylase activities were observed when tested at pH 5.4 and 6.2, and at 30-37 °C, except for Rhodotorula glacialis that showed elevated activity at 10-22 °C. In general, cellulase activity was high until pH 6.2 and between 22-37 °C, while the sample from Mrakia blollopis showed high activity at 4-22 °C. Peptide mass fingerprinting analysis of a potential amylase from Tetracladium sp. of about 70 kDa, showed several peptides with positive matches with glucoamylases from other fungi.
CONCLUSIONS
Almost all yeast species showed extracellular amylase or cellulase activity, and an inducing effect by the respective substrate was observed in a minor number of yeasts. These enzymatic activities were higher at 30 °C in most yeast, with highest amylase and cellulase activity in Tetracladium sp. and M. gelida, respectively. However, Rh. glacialis and M. blollopis displayed high amylase or cellulase activity, respectively, under 22 °C. In this sense, these yeasts are interesting candidates for industrial processes that require lower temperatures.
Topics: Amylases; Antarctic Regions; Cellulases; Fungal Proteins; Hydrogen-Ion Concentration; Temperature; Yeasts
PubMed: 26895625
DOI: 10.1186/s12866-016-0640-8 -
PloS One 2023The effects of filtration (F) and alpha-amylase depletion (AD) were assessed in n = 34 saliva samples. Each saliva sample was split into three aliquots and treated as...
The effects of filtration (F) and alpha-amylase depletion (AD) were assessed in n = 34 saliva samples. Each saliva sample was split into three aliquots and treated as follows: (1) no treatment; (2) 0.45μm commercial filter; and (3) 0.45μm commercial filter and affinity depletion of alpha-amylase. Then, a panel of biochemical biomarkers consisting of amylase, lipase, alanine aminotransferase (ALT), aspartate aminotransferase (AST), gamma-glutamyl transferase (GGT), alkaline phosphatase (ALP), creatine kinase (CK), calcium, phosphorus, total protein, albumin, urea, creatinine, cholesterol, triglycerides, and uric acid was measured. Differences between the different aliquots were observed in all measured analytes. The most marked changes were found in triglycerides and lipase data for filtered samples, and in alpha-amylase, uric acid, triglycerides, creatinine, and calcium results in alpha-amylase-depleted aliquots. In conclusion, the salivary filtration and amylase depletion methods employed in this report caused significant changes in saliva composition measurements. Based on these results, it would be recommended to consider the possible effects of these treatments in salivary biomarkers when filtration or amylase depletion is performed.
Topics: alpha-Amylases; Creatinine; Uric Acid; Calcium; Triglycerides; Biomarkers; Amylases
PubMed: 37235564
DOI: 10.1371/journal.pone.0286092