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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 -
British Journal of Hospital Medicine... Jan 2009
Topics: Abdominal Pain; Amylases; Diagnosis, Differential; Humans; Hyperamylasemia; Pancreatic Diseases
PubMed: 19357566
DOI: 10.12968/hmed.2009.70.Sup1.37706 -
Journal of Hospital Medicine May 2016
Review
Topics: Abdominal Pain; Acute Disease; Amylases; Humans; Pancreatitis
PubMed: 27160507
DOI: 10.1002/jhm.2544 -
Surgery Jul 2016Amylase was the first enzyme to be characterized, and for the previous 200 years, its clinical role has been restricted to a diagnostic aid. Recent interface research... (Review)
Review
BACKGROUND
Amylase was the first enzyme to be characterized, and for the previous 200 years, its clinical role has been restricted to a diagnostic aid. Recent interface research has led to a substantial expansion of its role into novel, viable diagnostic, and therapeutic applications to cancer, infection, and wound healing. This review provides a concise "state-of-the-art" overview of the genetics, structure, distribution, and localization of amylase in humans.
METHOD
A first-generation literature search was performed with the MeSH search string "Amylase AND (diagnost∗ OR therapeut$)" on OVIDSP and PUBMED platforms. A second-generation search was then performed by forward and backward referencing on Web of Knowledge™ and manual indexing, limited to the English Language.
RESULTS
"State of the Art" in amylase genetics, structure, function distribution, localisation and detection of amylase in humans is provided. To the 4 classic patterns of hyperamylasemia (pancreatic, salivary, macroamylasemia, and combinations) a fifth, the localized targeting of amylase to specific foci of infection, is proposed.
CONCLUSIONS
The implications are directed at novel therapeutic and diagnostic clinical applications of amylase such as the novel therapeutic drug classes capable of targeted delivery and "smart release" in areas of clinical need. Future directions of research in areas of high clinical benefit are reported.
Topics: Amylases; Humans
PubMed: 27117578
DOI: 10.1016/j.surg.2016.01.005 -
Medicine Jul 1976This review of the English literature on amylase was undertaken because no recent discussion of the subject could be located, no comprehensive list of disorders causing... (Review)
Review
This review of the English literature on amylase was undertaken because no recent discussion of the subject could be located, no comprehensive list of disorders causing hyperamylasemia or hyperamylasuria is available, and several major advances in the area have been made, notably the amylase isoenzyme determination and Cam/Ccr ratio. Several important concepts have emerged from this review. First, hyperamylasemia and hyperamylasuria are not specific indices of the presence of pancreatic disease or damage. Second, serum and urinary amylase levels can be spuriously normal with hypertriglyceridemia and pancreatitis. Third, the current emphasis on diagnostic methods for measuring serum amylase isoenzymes promises to improve the specificity of this determination. It will also enhance our understanding of the sources, distribution, metabolism, and elmination of amylase. Fourth, the development of the Cam/Ccr ratio may provide a practical diagnostic tool for separating clinically significant hyperamylasemia due to pancreatitis from that caused by other factors. Both the the isoamylase determination and Cam/Ccr ratio clearly require future research to place their clinical application in the proper perspective.
Topics: Amylases; Ascitic Fluid; Creatinine; Female; Humans; Pancreatitis; Pleural Effusion; Pregnancy; Triglycerides
PubMed: 781463
DOI: 10.1097/00005792-197607000-00001 -
Digestion 1975Hyperamylasaemia has long been regarded as pathognomonic of acute pancreatitis. However, recent work has revealed a number of conditions where a gross elevation may be... (Review)
Review
Hyperamylasaemia has long been regarded as pathognomonic of acute pancreatitis. However, recent work has revealed a number of conditions where a gross elevation may be an incidental finding, notably diabetic ketoacidosis. The recent discovery of 'macroamylase', a high molecular weight amylase-protein complex capable of producing hyperamylasaemia with low urine amylase, has further complicated diagnosis and has led to the introduction of the ratio of amylase clearance to creatinine clearance as a diagnostic aid. Serum amylase may be resolved, by most electrophoretic media, into bands which correspond to those obtained when pancreatic homogenates or saliva are electrophoresed. The initial promise of this technique has not been realised at the routine diagnostic level. Duodenal juice amylase has been the classical enzyme used in assessing exocrine pancreatic function and although it is still of value it is being amplified by other enzyme tests.
Topics: Acute Disease; Adult; Age Factors; Amylases; Animals; Child; Chronic Disease; Clinical Enzyme Tests; Female; Glycoside Hydrolases; Humans; Isoamylase; Macromolecular Substances; Male; Molecular Weight; Pancreatic Juice; Pancreatitis; Sex Factors
PubMed: 1104398
DOI: 10.1159/000197696 -
The New England Journal of Medicine Nov 1967
Topics: Amylases; Humans; Pancreatitis
PubMed: 6051040
DOI: 10.1056/NEJM196711022771810 -
Biotechnology and Applied Biochemistry Apr 2022By reducing the activation energy, enzymes accelerate the chemical reaction; therefore, they are good alternative for industrial catalysts. Amylase is a suitable enzyme... (Review)
Review
By reducing the activation energy, enzymes accelerate the chemical reaction; therefore, they are good alternative for industrial catalysts. Amylase is a suitable enzyme as a catalyst for the chemical decomposition of starch. This enzyme is of great importance, and its production is highly profitable. α-Amylase is among the most important amylases produced naturally by animals, plants, and microorganisms. Still, the α-amylases produced by bacteria have a special place in industry and commerce. Moreover, a large volume of this enzyme can be produced by selecting an appropriate and optimized host to clone and express the α-amylase gene. The present study briefly reviews the structure, application, sources, and hosts used to produce recombinant α-amylase.
Topics: Amylases; Animals; Bacteria; Starch; alpha-Amylases
PubMed: 33655550
DOI: 10.1002/bab.2140 -
Extremophiles : Life Under Extreme... May 2021α-Amylase is the most significant glycoside hydrolase having applications in various industries. It cleaves the α,1-4 glucosidic linkages of polysaccharides like... (Review)
Review
α-Amylase is the most significant glycoside hydrolase having applications in various industries. It cleaves the α,1-4 glucosidic linkages of polysaccharides like starch, glycogen to yield a small polymer of glucose in α-anomeric configuration. α-Amylase is produced by all the three domains of life but microorganisms are preferred sources for industrial-scale production due to several advantages. Enormous studies and research have been done in this field in the past few decades. Still, it is requisite to work on enzyme stability and catalysis, as it loses its functionality in extreme. As the enzyme loses its structural and catalytic property under extreme environmental conditions, it is mandatory to confer some potential strategies for enhancing enzyme behaviour in such conditions. This limitation of an enzyme can be overcome up to some extent by extremophiles. They serve as an excellent source of α-amylase with outstanding features. This review is an attempt to encapsulate some structure-based strategies for improving enzyme behaviour thereby enabling researchers to selectively amend any of the strategies as per requirement during upstream and downstream processing for higher enzyme yield and stability. Thus, it will provide some cutting-edge strategies for tailoring α-amylase producing organism and enzyme with the help of several computational biology tools.
Topics: Amylases; Catalysis; Computational Biology; Extremophiles; alpha-Amylases
PubMed: 33754213
DOI: 10.1007/s00792-021-01223-2 -
Acta Universitatis Carolinae. Medica.... 1987Total amylase activity in serum and urine is formed by pancreatic (P) and salivary (S) isoenzymes. The evaluation of isoamylases provides better information on enzyme... (Review)
Review
Total amylase activity in serum and urine is formed by pancreatic (P) and salivary (S) isoenzymes. The evaluation of isoamylases provides better information on enzyme changes during the disease than total activities alone. The resolution of pancreatic from extrapancreatic origin of hyperamylasemia may be clinically important. The experience obtained from the analysis of isoamylases in more than 1500 patients with different clinical diagnoses we compare with a contemporary knowledge of disturbances in amylase activities. We developed a method separating quantitatively both isoamylases on the mini-columns of ion-exchanger which we used in routine clinical investigation. In the first section we selected the findings on physiology and biochemistry of isoamylases. We described for the first time a significant decrease of P-isoamylase activity in serum during the intravenous infusions of hypertonic glucose, amino acids and during acute hypercalcaemia. We suggested that hypertonic glucose, amino acids and calcium may regulate directly or indirectly the amylase flux from acinar cells in the pancreas across basolateral membrane into blood. This endocrine secretion of amylase may be important in different clinical conditions in which changes of neurohumoral and/or hormonal regulation are developed. The isoamylase activities in patients with different diagnosis are analyzed in the clinical section. The results may be correctly evaluated only in connection with the pathogenesis of isoamylase changes. Disorders of the organs producing amylase (i.e. pancreas or salivary glands) may induce changes of isoamylases depending on their functional status. A progressive loss of amylase producing cells may be accompanied by a decrease of enzyme activity in serum as was described in chronic pancreatitis with exocrine insufficiency. However, the amylase activity in serum is significantly influenced by clearance mechanisms, too. Disorders of the liver or kidneys are accompanied predominantly with hyperamylasemia caused by the disturbed clearance mechanisms. The amylase activity in serum is a consequence of the result between input and output of the enzyme within the blood stream. Some humoral and hormonal regulations are able to modulate both processes in vivo. We suppose that pathogenetic standpoint has the main role for correct interpretation of isoamylase activities. The pathogenesis of hyperamylasemia is therefore discussed in single chapters. In conclusion, the isoamylase activities in serum and urine are influenced beside genetic background by many factors in health and disease which may be respected during the evaluation of the results.
Topics: Amylases; Disease; Humans; Isoenzymes
PubMed: 2446482
DOI: No ID Found