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Academic literature on the topic 'Amylases'

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Published: 4 June 2021
Last updated: 4 March 2023

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Journal articles on the topic "Amylases"

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Sachdev, Shivani, Sanjay Kumar Ojha, and Snehasish Mishra. "Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application." International Journal of Applied Sciences and Biotechnology 4, no. 1 (March 31, 2016): 3–14. http://dx.doi.org/10.3126/ijasbt.v4i1.14574.

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Amylase is one of the leading enzymes used in industry from decades. The preliminary function of this enzyme is the hydrolysis of the starch molecule into glucose units and oligosaccharides. Amylases have spectacular application in broad spectrum of industries such as food, detergent, pharmaceutical and fermentation industries. Among different type of amylases α- amylase is in utmost demand because of its striking features. This particular enzyme is a good substitute over the chemicals catalyst used in industries. α- amylases can be acquired from different sources such as microorganism, animals and plants. Microorganisms are the major source of production of amylase because of the ease of availability, manipulation and operation. The starch converting enzymes is basically generated using submerged fermentation. Some of the prominent characteristics of amylase are its mode of action, substrate specificity and operating condition (temperature and pH). Amylases from different bacterial sources contribute differently to the particular trait of the enzyme. Bacillus amylases have been studied and applied so far because of their robustness in nature and easy accessible pure form of it. Thus this makes it more specific and fit for distinct application in the industry. The purpose of this manuscript was the comparative analysis of the physical and chemical features of α amylases from Bacillus species. It also focuses on the unique characteristics of this enzyme and their industrial applications.Int J Appl Sci Biotechnol, Vol 4(1): 3-14
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Janeček, Štefan. "Amylolytic enzymes - focus on the alpha-amylases from Archae and plants." Nova Biotechnologica et Chimica 9, no. 1 (November 29, 2021): 5–26. http://dx.doi.org/10.36547/nbc.1284.

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Amylolytic enzymes represent a group of starch hydrolases and related enzymes that are active towards the α-glycosidic bonds in starch and related poly- and oligosaccharides. The three best known amylolytic enzymes are α-amylase, β-amylase and glucoamylase that, however, differ from each other by their amino acid sequences, three-dimensional structures, reaction mechanisms and catalytic machineries. In the sequence-based classification of all glycoside hydrolases (GHs) they have therefore been classified into the three independent families: GH13 (α-amylases), GH14 (β-amylases) and GH15 (glucoamylases). Some amylolytic enzymes have been placed to the families GH31 and GH57. The family GH13 together with the families GH70 and GH77 constitutes the clan GH-H, well-known as the α-amylase family. It contains more than 6,000 sequences and covers 30 various enzyme specificities sharing the conserved sequence regions, catalytic TIM-barrel fold, retaining reaction mechanism and catalytic triad. Among the GH13 α-amylases, those produced by plants and archaebacteria exhibit common sequence similarities that distinguish them from the α-amylases of the remaining taxonomic sources. Despite the close evolutionary relatedness between the plant and archaeal α-amylases, there are also specific differences that discriminate them from each other. These specific differences could be used in an effort to reveal the sequence-structural features responsible for the high thermostability of the α-amylases from Archaea.
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Türker, Celal, and Bahri Devrim Özcan. "Alfa-amilaz Enzimlerini Üreten Termofilik Bacillus Suşlarının İzolasyonu ve Enzimlerin Kısmi Karakterizasyonu." Turkish Journal of Agriculture - Food Science and Technology 3, no. 6 (March 7, 2015): 387. http://dx.doi.org/10.24925/turjaf.v3i6.387-393.312.

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In the present study, we isolated three thermophilic Bacillus strains from the soil samples collected from the coast sediments of the Burnaz Stream located in Erzin. The isolates were entitled as Bacillus sp. CT1, CT2, and CT3, respectively. The maximum α-amylase production was revealed at 60°C for CT1 strain, and at 80°C for CT2 and CT3 strains, respectively. The optimum enzyme activity was observed at 90°C for CT1 α-amylase, whereas at 60°C for CT2 and CT3 α-amylases. On the other hand, optimum pH value for CT2 α-amylase was 7.0, whereas 8.0 for CT1 and CT3 α-amylases. The specific activities of CT1, CT2, and CT3 amylases were 317.6, 113.3 and 362.7 U/mg at 55°C, respectively. The estimated molecular weight of CT1 and CT3 α-amylase was 65 kDa, and for CT2 α-amylase was 38 kDa by zymogram analysis.
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Sondhi, Sonica, Palki Sahib Kaur, Himansi Sura, Manisha Juglani, and Deepali Sharma. "Amylase Based Clarification of Apple, Orange and Grape Juice." CGC International Journal of Contemporary Technology and Research 3, no. 2 (July 17, 2021): 187–90. http://dx.doi.org/10.46860/cgcijctr.2021.06.31.187.

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Amylases are starch-degrading enzymes produced by many bacteria, plants, fungi and animals. It has found tremendous application in industry. One of its applications is in fruit industry wherein amylases are used to clarify fruit juices and reduce its viscosity. In fruits, high amount of starch is present which resulted in increased viscosity of the prepared juices. This may also lead to settling of juice at bottom. Amylases act on starch component and degrade it. In the current study, amylase from B. licheniformis was used for the clarification of apple, orange and grape juices. Total suspended solids, viscosity and total acidity was found to decrease with increasing amylase concentration. The results revealed that after amylase treatment the color, texture and flavor of juices were also improved.
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Roth, Christian, Olga V. Moroz, Johan P. Turkenburg, Elena Blagova, Jitka Waterman, Antonio Ariza, Li Ming, et al. "Structural and Functional Characterization of Three Novel Fungal Amylases with Enhanced Stability and pH Tolerance." International Journal of Molecular Sciences 20, no. 19 (October 3, 2019): 4902. http://dx.doi.org/10.3390/ijms20194902.

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Amylases are probably the best studied glycoside hydrolases and have a huge biotechnological value for industrial processes on starch. Multiple amylases from fungi and microbes are currently in use. Whereas bacterial amylases are well suited for many industrial processes due to their high stability, fungal amylases are recognized as safe and are preferred in the food industry, although they lack the pH tolerance and stability of their bacterial counterparts. Here, we describe three amylases, two of which have a broad pH spectrum extending to pH 8 and higher stability well suited for a broad set of industrial applications. These enzymes have the characteristic GH13 α-amylase fold with a central (β/α)8-domain, an insertion domain with the canonical calcium binding site and a C-terminal β-sandwich domain. The active site was identified based on the binding of the inhibitor acarbose in form of a transglycosylation product, in the amylases from Thamnidium elegans and Cordyceps farinosa. The three amylases have shortened loops flanking the nonreducing end of the substrate binding cleft, creating a more open crevice. Moreover, a potential novel binding site in the C-terminal domain of the Cordyceps enzyme was identified, which might be part of a starch interaction site. In addition, Cordyceps farinosa amylase presented a successful example of using the microseed matrix screening technique to significantly speed-up crystallization.
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Melo, Francislete R., Mauricio P. Sales, Lucilene S. Pereira, Carlos Bloch, Octavio L. Franco, and Maria B. Ary. "α-Amylase Inhibitors from Cowpea Seeds." Protein & Peptide Letters 6, no. 6 (December 1999): 385–90. http://dx.doi.org/10.2174/092986650606221117144709.

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Abstract: This work describes the first isolation and partial characterization of α-amylase inhibitors from cowpea (Vigna unguiculata) seeds. α-Amylase inhibitors were isolated using an affinity chromatography on Red Sepharose CL-6B. The bound Red Sepharose fraction was active against α-amylases from Bacillus sp., Aspergilus oryzae, V unguicu/ata seeds and also against α-amylases from Callosobruchus maculatus larvae.
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Garba, L., M. M. Ibrahim, E. K. Sahara, M. T. Adamu, S. Isa, and A. A. Yarma. "Preliminary Investigation of Amylase Producing-Bacteria from Soil in Gombe Metropolis." Journal of Environmental Bioremediation and Toxicology 4, no. 1 (July 30, 2021): 1–3. http://dx.doi.org/10.54987/jebat.v4i1.576.

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Amylases are enzymes that are able to hydrolyse starch or glycogen molecules into polymers of glucose units. They have great potential applications in various industrial processes like in pharmaceutical, fermentation and food industries. Research on starch degrading enzymes has resulted into increased applications of amylases in different industrial processes. These enzymes occupy a greater space in the current biotechnological processes such as detergent, starch degradation, pharmaceutical, foodstuff, textile, and paper manufacturing. In fact, amylases constitute nearly 25% of the total sale of global enzymes. Amylases have been screened and identified from various sources, both eukaryotic and prokaryotic organisms such as animals, plants, fungi and bacteria, respectively. To further isolate novel amylases with enhanced desirable properties for such diverse industrial application, more organisms need to be screened. In this study, a total of 27 bacterial isolates were isolated from soil samples in Gombe metropolis. The bacteria were screened for amylase production using plate screening method. Each isolate was streaked onto a 1% starch agar plate and incubated for 24h at 37 °C. The plates were covered with iodine solution and observed for positive amylase isolates based on the formation of clearing zones against the blue black background. The results confirmed eight (8) isolates of amylase-producing bacteria which include Bacillus subtilis, Escherichia coli, Streptococcus spp., Salmonella spp., Pseudomonas spp., Serratia spp., Proteus vulgaris, and Klebsiella spp. In conclusion, bacterial isolates capable of amylase production have been successfully screened and identified. This research may serve as a stepping stone to isolating functional amylase enzymes from these bacteria for promising industrial applications.
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Marengo, Mauro, Davide Pezzilli, Eleonora Gianquinto, Alex Fissore, Simonetta Oliaro-Bosso, Barbara Sgorbini, Francesca Spyrakis, and Salvatore Adinolfi. "Evaluation of Porcine and Aspergillus oryzae α-Amylases as Possible Model for the Human Enzyme." Processes 10, no. 4 (April 15, 2022): 780. http://dx.doi.org/10.3390/pr10040780.

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α-amylases are ubiquitous enzymes belonging to the glycosyl hydrolase (GH13) family, whose members share a high degree of sequence identity, even between distant organisms. To understand the determinants of catalytic activity of α-amylases throughout evolution, and to investigate the use of homologous enzymes as a model for the human one, we compared human salivary α-amylase, Aspergillus oryzae α-amylase and pancreatic porcine α-amylase, using a combination of in vitro and in silico approaches. Enzyme sequences were aligned, and structures superposed, whereas kinetics were spectroscopically studied by using commercial synthetic substrates. These three enzymes show strikingly different activities, specifically mediated by different ions, despite relevant structural homology. Our study confirms that the function of α-amylases throughout evolution has considerably diverged, although key structural determinants, such as the catalytic triad and the calcium-binding pocket, have been retained. These functional differences need to be carefully considered when α-amylases, from different organisms, are used as a model for the human enzymes. In this frame, particular focus is needed for the setup of proper experimental conditions.
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Urdal, P., S. Landaas, P. Kierulf, and J. H. Strømme. "Macroamylase immunoglobulins show high affinity for animal and human amylases." Clinical Chemistry 31, no. 5 (May 1, 1985): 699–702. http://dx.doi.org/10.1093/clinchem/31.5.699.

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Abstract We have examined the affinity shown by the immunoglobulin fraction from each of five sera containing macroamylase for amylases from different sources: human saliva or human, porcine, or ovine pancreas. High affinity constants, 0.4 X 10(10) to 7.2 X 10(10) L/mol, were found in competitive binding experiments with human or porcine pancreatic amylase. All but one serum yielded linear Scatchard plots, indicating that in most sera the amylase-binding immunoglobulins are homogeneous, possibly monoclonal. The immunoglobulin fractions from different sera differed in their specificity: two of them bound all four types of amylases, whereas two bound only one type. Three of the five immunoglobulin fractions showed considerably higher affinity towards one or both of the animal amylases than towards the human ones, and may be primarily directed against some animal amylase.
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Domingues, Claudia M., and Rosane M. Peralta. "Production of amylase by soil fungi and partial biochemical characterization of amylase of a selected strain (Aspergillus fumigatus Fresenius)." Canadian Journal of Microbiology 39, no. 7 (July 1, 1993): 681–85. http://dx.doi.org/10.1139/m93-098.

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Filamentous fungi from soil were screened for their ability to produce amylases in semisolid and liquid media with wheat bran. A selected strain identified as Aspergillus fumigatus Fresenius showed high enzymatic activity for α-amylase and glucoamylase. The maximal yield of these amylases was obtained when lignocellulosic materials were the carbon sources. The optimal pH and temperature were 6.0 and 50 °C, respectively, for both enzymes. α-Amylase activity was more thermostable than glucoamylase activity.Key words: amylolitic fungi, α-amylase, glucoamylase, Aspergillus fumigatus.
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Dissertations / Theses on the topic "Amylases"

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Charuel, Jean-Luc. "Amylases et tumeurs." Paris 5, 1991. http://www.theses.fr/1991PA05P082.

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Ramachandran, Nivetha. "Development of improved [alpha]-amylases /." Link to the online version, 2005. http://hdl.handle.net/10019.1/1102.

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Ramachandran, Nivetha. "Development of improved α-amylases." Thesis, Stellenbosch : University of Stellenbosch, 2005. http://hdl.handle.net/10019.1/1102.

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Thesis (DSc (Microbiology))--University of Stellenbosch, 2005.
The technological advancement of modern human civilisation has, until recently, depended on extensive exploitation of fossil fuels, such as oil, coal and gas, as sources of energy. Over the last few decades, greater efforts have been made to economise on the use of these nonrenewable energy resources, and to reduce the environmental pollution caused by their consumption. In a quest for new sources of energy that will be compatible with a more sustainable world economy, increased emphasis has been place on researching and developing alternative sources of energy that are renewable and safer for the environment. Fuel ethanol, which has a higher octane rating than gasoline, makes up approximately two-thirds of the world’s total annual ethanol production. Uncertainty surrounding the longterm sustainability of fuel ethanol as an energy source has prompted consideration for the use of bioethanol (ethanol from biomass) as an energy source. Factors compromising the continued availability of fuel ethanol as an energy source include the inevitable exhaustion of the world’s fossil oil resources, a possible interruption in oil supply caused by political interference, the superior net performance of biofuel ethanol in comparison to gasoline, and a significant reduction in pollution levels. It is to be expected that the demand for inexpensive, renewable substrates and cost-effective ethanol production processes will become increasingly urgent. Plant biomass (including so-called ‘energy crops’, agricultural surplus products, and waste material) is the only foreseeable sustainable source of fuel ethanol because it is relatively low in cost and in plentiful supply. The principal impediment to more widespread utilisation of this important resource is the general absence of low cost technology for overcoming the difficulties of degrading the recalcitrant polysaccharides in plant biomass to fermentable sugars from ethanol can be produced. A promising strategy for dealing with this obstacle involves the genetic modification of Saccharomyces cerevisiae yeast strains for use in an integrated process, known as direct microbial conversion (DMC) or consolidated bioprocessing (CBP). This integrated process differs from the earlier strategies of SHF (separate hydrolysis and fermentation) and SSF (simultaneous saccharification and fermentation, in which enzymes from external sources are used) in that the production of polysaccharide-degrading enzymes, the hydrolysis of biomass and the fermentation of the resulting sugars to ethanol all take place in a single process by means of a polysaccharidefermenting yeast strain. The CBP strategy offers a substantial reduction in cost if S. cerevisiae strains can be developed that possess the required combination of substrate utilisation and product formation properties. S. cerevisiae strains with the ability to efficiently utilise polysaccharides such as starch for the production of high ethanol yields have not been described to date. However, significant progress towards the development of such amylolytic strains has been made over the past decade. With the aim of developing an efficient starch-degrading, high ethanol-yielding yeast strain, our laboratory has expressed a wide variety of heterologous amylase-encoding genes in S. cerevisiae. This study forms part of a large research programme aimed at improving these amylolytic ‘prototype’ strains of S. cerevisiae. More specifically, this study investigated the LKA1- and LKA2-encoded α-amylases (Lka1p and Lka2p) from the yeast Lipomyces kononenkoae. These α-amylases belong to the family of glycosyl hydrolases (EC 3.2.1.1) and are considered to be two of the most efficient raw-starch-degrading enzymes. Lka1p functions primarily on the α-1,4 linkages of starch, but is also active on the α-1,6 linkages. In addition, it is capable of degrading pullulan. Lka2p acts on the α-1,4 linkages. The purpose of this study was two-fold. The first goal was to characterise the molecular structure of Lka1p and Lka2p in order to better understand the structure-function relationships and role of specific amino acids in protein function with the aim of improving their substrate specificity in raw starch hydrolysis. The second aim was to determine the effect of yeast cell flocculence on the efficiency of starch fermentation, the possible development of high-flocculating, LKA1-expressing S. cerevisiae strains as ‘whole-cell biocatalysts’, and the production of high yields of ethanol from raw starch. In order to understand the structure-function relationships in Lka1p and Lka2p, standard computational and bioinformatics techniques were used to analyse the primary structure. On the basis of the primary structure and the prediction of the secondary structure, an N-terminal region (1-132 amino acids) was identified in Lka1p, the truncation of which led to the loss of raw starch adsorption and also rendered the protein less thermostable. Lka1p and Lka2p share a similar catalytic TIM barrel, consisting of four highly conserved regions previously observed in other α-amylase members. Furthermore, the unique Q414 of Lka1p located in the catalytic domain in place of the invariant H296 (TAKA amylase), which offers transition state stabilisation in α-amylases, was found to be involved in the substrate specificity of Lka1p. Mutational analysis of Q414 performed in the current study provides a basis for understanding the various properties of Lka1p in relation to the structural differences observed in this molecule. Knowing which molecular features of Lka1p contribute to its biochemical properties provides us with the potential to expand the substrate specificity properties of this α-amylase towards more effective processing of its starch and related substrates. In attempting to develop ‘whole-cell biocatalysts’, the yeast’s capacity for flocculation was used to improve raw starch hydrolysis by S. cerevisiae expressing LKA1. It was evident that the flocculent cells exhibited physicochemical properties that led to a better interaction with the starch matrix. This, in turn, led to a decrease in the time interval for interaction between the enzyme and the substrate, thus facilitating faster substrate degradation in flocculent cells. The use of flocculation serves as a promising strategy to best exploit the expression of LKA1 in S. cerevisiae for raw starch hydrolysis. This thesis describes the approaches taken to investigate the molecular features involved in the function of the L. kononenkoae α-amylases, and to improve their properties for the efficient hydrolysis of raw starch. This study contributes to the development of amylolytic S. cerevisiae strains for their potential use in single-step, cost-effective production of fuel ethanol from inexpensive starch-rich materials.
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Nahoum, Virginie. "Alpha-amylases de mammifères et d'insectes, relation structure/fonction." Aix-Marseille 3, 2000. http://www.theses.fr/2000AIX30010.

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Les -amylases (-1,4-glucan-4-glucanohydrolase, ec 3. 2. 1. 1) catalysent l'hydrolyse des liaisons -(1,4) glycosidiques des composes de l'amidon. Dans cette these je presente l'analyse structurale de deux classes d'enzymes, les -amylases de mammiferes et d'insectes. Malgre l'abondance de donnees biochimiques sur ces complexes, les complexes entre l'-amylase humaine et des oligosaccharides avaient echappe a toute caracterisation structurale. Dans cette etude les structures cristallographiques de l'-amylase pancreatique humaine (hpa) en complexe avec des inhibiteurs naturels ont ete resolues. Le tetrasaccharide acarbose et un pseudo-pentasccharide appartenant a la famille des trestatines ont montre des densites electroniques continues similaires correspondant a un pentasaccharide, occupant les sous-sites 3 a +2 de l'enzyme, et probablement resultant d'une transglycosylation. La fixation du cur acarviosine lie a une unite glucose aux sous-sites 1 a +2 apparait etre une etape critique du processus d'interaction entre les -amylases et les inhibiteurs derives des trestatines. Deux formes cristallines du complexe entre hpa et un inhibiteur proteique (-ai) issu du grain de haricot phaseolus vulgaris, obtenues a differents ph, ont ete resolues. La boucle flexible, typique des -amylases de mammiferes, montre deux conformations differentes, suggerant une sensibilite de cette boucle au ph. Une information structurale est procuree pour le residu arg 74 qui n'etait pas visible dans les precedentes analyses structurales. L'-amylase de la larve de tenebrio molitor (tma) a ete cristallisee en complexe avec l'inhibiteur -ai. Tma presente la structure commune aux -amylases, de grandes differences avec les -amylases de mammiferes se produisant dans les boucles. Malgre ces differences dans les boucles impliquees dans l'interaction, l'inhibiteur du haricot est capable d'inhiber a la fois les -amylases de mammiferes et d'insectes. La boucle flexible des -amylases de mammiferes, tronquee dans l'-amylase d'insecte montre une conformation differente dans les structures de tma native et de tma en complexe avec -ai. La modelisation de l'attachement des isoformes de -ai dans le site actif de differentes -amylases jette un regard sur la specificite de ces inhibiteurs.
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Talamond, Pascale. "Etude de l' α-amylase de lactobacillus fermentum : purification, caractérisation et propriétés. Comparaison avec les α-amylases de Lb. Plantarum et Lb. Manihotivorans." Aix-Marseille 3, 2002. http://www.theses.fr/2002AIX30087.

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Une nouvelle a-amylase de Lb. Fermentum (FERMENTA) obtenue par fermentation à partir de céréales a été purifiée, étudiée au niveau structural et fonctionnel et comparée avec deux autres a-amylases de Lb. Plantarum (PLANTAA) et de Lb. Manihotivorans (MANIHOA). Les trois a-amylases présentent une masse moléculaire voisinant les 100 kDa et des pI du même ordre de grandeur (3,5±0,3). Comme PLANTAA et MANIHOA, la structure de FERMENTA contient des séquences répétées en C-terminal. Les propriétés physico-chimiques (pH 5 et température 40ʿC) ont été déterminées et l'étude cinétique avec l'amylose pour substrat et l'acarbose pour inhibiteur a été effectuée. L'inhibition non-compétitive mixte pour FERMENTA (K1i = 5,3 æM et L1i = 1,7 æM) et incompétitive pour PLANTAA et MANIHOA révèlent que l'acarbose est un puissant inhibiteur pour ces trois a-amylases. Ces études cinétiques montrent l'existence d'un site secondaire de fixation des carbohydrates distinct du site actif et nécessaire pour l'hydrolyse des substrats longs
A new a-amylase from Lactobacillus fermentum (FERMENTA) was purified. The structural and functional characteristics were studied and compared with Lb. Plantarum (PLANTAA) and Lb. Manihotivorans (MANIHOA) a-amylases. FERMENTA molecular mass (100 kDa) is in the same range than those determined for PLANTAA and MANIHOA. Structure of FERMENTA indicates that the sequence contains two equal parts with the C-terminal repeats. Isoelectric point of the three a-amylases are about the same (3. 5). The functional properties of FERMENTA are studied : optimal pH (5. 0) and temperature (40ʿC). Kinetics of the three a-amylases with amylose and acarbose were carried out. Inhibition of FERMENTA is of mixed noncompetitive type while the inhibition of PLANTAA and MANIHOA is of uncompetitive type. Whatever the inhibition type, acarbose is a strong inhibitor of these amylases. These results indicate that they contain, in addition to the active site, a soluble carbohydrate (substrate or product) binding site
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Rumbak, Elaine. "The cloning and characterization of an α-amylase and a branching enzyme from Butyrivibrio fibrisolvens H17c and their expression in Escherichia coli." Doctoral thesis, University of Cape Town, 1991. http://hdl.handle.net/11427/22555.

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Bibliography: pages 145-172.
Butyrivibrio fibrisolvens H17c is an important anaerobic bacterium found in the rumen of most ruminants. The aim of this thesis was to establish a genebank of B. fibrisolvens H17c DNA in E.coli and to isolate and characterize genes encoding enzymes involved in the degradation of the major plant polysaccharides. A library of chromosomal DNA fragments from B. fibrisolvens was established in the E. coli-Bacillus subtilis shuttle vector pEBl. The library was screened for the expression of B. fibrisolvens genes in E. coli. E. coli clones expressing glutamine synthetase, carboxymethylcellulase, β-glucosidase and amylolytic-type activities were isolated. A gene (amyA) expressing amylolytic activity and encoding an α-amylase was located on a 5.0 kb DNA fragment and expressed from its own promoter in E. coli. It was shown that more than 86% of the amylolytic actvity was located in the periplasm of the E.coli host and TnphoA mutagenesis indicated the presence of a functional signal peptide. The nucleotide sequence of amyA was determined and encoded a protein of 976 amino acids with a calculated Mr of 106,964. High sequence similarity was demonstrated between the B. fibrisolvens α-amylase and other α-amylases in the three highly conserved regions which constitute the active centre. Conserved regions were all located in the N-terminal half of the B. fibrisolvens amylase and no homology to other amylases was detected for the remainder of the protein. Approximately 40% of the C-terminal region of the protein could be deleted without loss of enzymatic activity. The B. fibrisolvens α-amylase degraded amylose, amylopectin and soluble starch with maltotriose as the major initial hydrolysis product. A gene (glgB) encoding a glycogen branching enzyme, the activity of which produced clearing on starch azure plates, was isolated. The glgB gene was expressed from its own promoter in the host E.coli and encoded a protein of 639 amino acids with a calculated Mr of 73,875. The deduced amino acid sequence of the glgB gene showed high sequence homology (46-50%) to other branching enzymes. The branching enzyme was purified to homogeneity and the properties of the purified enzyme were investigated. Optimal activity of the branching enzyme was at pH 7.2 and 37°C. The branching enzyme was shown to transfer chains of between 5 to 10 glucose units using α-1,4 glucans as substrates, and to stimulate the "de novo" synthesis of a polysaccharide similar to glycogen.
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Cottaz, Sylvain. "Synthèses chimiques et enzymatiques de maltodextrines modifiées : étude du centre actif de la cyclodextrine-glucosyltransférase." Grenoble 1, 1989. http://www.theses.fr/1989GRE10136.

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Des enzymes de la super-famille des amylases peuvent etre etudiees par la methode aux analogues de substrat. Les thiomaltodextrines lineaires et cycliques ont ete obtenues par synthese chimique. Les syntheses enzymatiques de nouveaux substrats specifiques des alpha-amylases ont ete realisees soit par esterification de maltodextrines, soit par reaction de couplage avec une cyclodextrine modifiee catalysee par la cyclodextrine-glucosyltransferase (cgtase). L'utilisation par la cgtase de fluorures de maltosyle modifies a apporte de nouvelles informations sur la specificite de son centre actif, et permis la synthese de cyclodextrines modifiees
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Pan, Oscar Chi-Chien. "In search of peptide inhibitors for alpha-amylases." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0027/MQ51441.pdf.

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LECOMMANDEUR, DIDIER. "Etude moleculaire des alpha-amylases de differentes cereales." Paris 6, 1989. http://www.theses.fr/1989PA066295.

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Une etude comparative des alpha-amylases de grains en germination de plusieurs cereales a ete effectuee. Un microdosage specifique utilise comme substrat le benzilidene p-nitrophenyl maltoheptaoside. Les alpha-amylases de mais, sorgho, avoine et riz ont ete purifiees par precipitation au glycogene et chromatographie d'interaction hydrophobe, les deux isoformes de l'alpha-amylase d'orge parchromatofocalisation et chromatographie d'affinite. Une caracterisation immunochimique, utilisant les reactions croisees avec des anticorps polyclonaux anti-alpha-amylase 1 et anti-alpha-amylase 2 d'orge, montre que chez l'avoine et le sorgho deux antigenes sont presents, et trois chez le mais. Leurs tailles sont voisines (43000 a 47000). Les alpha-amylases d'orge, de sorgho et d'avoine ne semblent pas glycosylees. Une forme de l'alpha-amylase de mais est o-glycosylee. La n-glycosylation de l'alpha-amylase de riz produit, a partir de deux polypeptides de taille differente, des glycoproteines de meme taille. Sept anticorps monoclonaux anti-alpha-amylase 1 d'orge ont ete produits et caracterises. Six sont specifiques de cette forme, le spetieme reconnait egalement la forme 2. Certains anticorps reconnaissent des alpha-amylases de riz, mais ou sorgho
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Valantin-Rollet, Carole. "Etude du non parallélisme de la composition en 4 hydrolases digestives du pancréas de rat et de sa sécrétion : influence de la synthèse, du "turnover", du transport et de l'excrétion : effets de l'âge et d'une malnutrition protéique (...) suivie." Dijon, 1985. http://www.theses.fr/1985DIJOS015.

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Books on the topic "Amylases"

1

Amylase Research Society of Japan., ed. Enzyme chemistry and molecular biology of amylases and related enzymes. Boca Raton: CRC Press, 1995.

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Galich, I. P. Amilazy mikroorganizmov. Kiev: Nauk. dumka, 1987.

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Duff, Bernard. Studies on the alpha-glucosidase of Candida Fennica CBS 5928. Dublin: University College Dublin, 1996.

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Amylase Research Society of Japan., ed. Handbook of amylases and related enzymes: Their sources, isolation methods, properties and applications. Oxford: Pergamon Press, 1988.

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Lauro, Marianna. [Alpha]-amylolysis of barley starch. Espoo [Finland]: Technical Research Centre of Finland, 2001.

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1940-, Ōnishi Masatake, ed. Glycoenzymes. Tokyo: Japan Scientific Societies Press, 2000.

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Spreinat, Andreas. Isolierung, Charakterisierung und Synergismus der Pullulanasen und [alpha]-Amylase aus Clostridium thermosulfurogenes EM1. Göttingen: Unitext, 1991.

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Škrha, Jan. Clinical significance of amylase isoenzyme determination. Praha: Univerzita Karlova, 1987.

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Keating, Lisa Ann. Studies on the amylolytic system of Bacillus coagulans. Dublin: University College Dublin, 1996.

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Heupke, Hans-Jürgen. [Alpha]-Amylase-Synthese und -Sekretion in Aleuronzellen der Gerste (Hordeum vulgare L.): Untersuchungen zur Beteiligung des Golgiapparates am intrazellulären Transport. Konstanz: Hartung-Gorre, 1988.

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Book chapters on the topic "Amylases"

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Satyanarayana, T., J. L. Uma Maheswar Rao, and M. Ezhilvannan. "α-Amylases." In Enzyme Technology, 189–220. New York, NY: Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-35141-4_10.

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Samanta, Saptadip. "α-Amylases." In Microbial Fermentation and Enzyme Technology, 13–39. Boca Raton : CRC Press, [2020]: CRC Press, 2020. http://dx.doi.org/10.1201/9780429061257-2.

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Jensen, B., and J. Olsen. "Amylases and Their Industrial Potential." In Thermophilic Moulds in Biotechnology, 115–37. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-015-9206-2_5.

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Svensson, B., M. R. Sierks, H. Jespersen, and M. Søgaard. "Structure—Function Relationships in Amylases." In Biotechnology of Amylodextrin Oligosaccharides, 28–43. Washington, DC: American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0458.ch003.

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Fogarty, William M., and Catherine T. Kelly. "Recent Advances in Microbial Amylases." In Microbial Enzymes and Biotechnology, 71–132. Dordrecht: Springer Netherlands, 1990. http://dx.doi.org/10.1007/978-94-009-0765-2_3.

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Hopkins, R. H. "The actions of the amylases." In Advances in Enzymology - and Related Areas of Molecular Biology, 389–414. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122518.ch9.

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Cowieson, Aaron J., Laerke T. Haahr, and Lars K. Skov. "Starch- and protein-degrading enzymes in non-ruminant animal production." In Enzymes in farm animal nutrition, 89–102. 3rd ed. Wallingford: CABI, 2022. http://dx.doi.org/10.1079/9781789241563.0006.

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Abstract This chapter describes the characteristics, mode of action, in vivo responses, variability of effect and factors that may be considered when exploring the usefulness of exogenous amylases and proteinases in animal feeds.
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Balakrishnan, Divya, Swaroop S. Kumar, and Shiburaj Sugathan. "Amylases for Food Applications—Updated Information." In Energy, Environment, and Sustainability, 199–227. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-3263-0_11.

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El-Enshasy, Hesham A., Yasser R. Abdel Fattah, and Nor Zalina Othman. "Amylases: Characteristics, Sources, Production, and Applications." In Bioprocessing Technologies in Biorefinery for Sustainable Production of Fuels, Chemicals, and Polymers, 111–30. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118642047.ch7.

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Bhatt, Bhumi M., Ujjval B. Trivedi, and Kamlesh C. Patel. "Extremophilic Amylases: Microbial Production and Applications." In Microorganisms for Sustainability, 185–205. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-1710-5_7.

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Conference papers on the topic "Amylases"

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Condruc, Viorica. "METHODS FOR ORIENTED SYNTHESIS OF EXOCELLULAR AMYLASES USING FUNGAL STRAIN Aspergillus niger CNMN FD 06." In XIth International Congress of Geneticists and Breeders from the Republic of Moldova. Scientific Association of Geneticists and Breeders of the Republic of Moldova, Institute of Genetics, Physiology and Plant Protection, Moldova State University, 2021. http://dx.doi.org/10.53040/cga11.2021.124.

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Curvelo Santana, José Carlos, Joana Paula Menezes Biazus, Roberto Rodrigues de Souza, and ELIAS BASILE TAMBOURGI. "ION-EXCHANGE EFFECT ON THE PURIFICATION OF AMYLASES FROM MAIZE MALT BY EXPANDED BED ADSORPTION." In Simpósio Nacional de Bioprocessos e Simpósio de Hidrólise Enzimática de Biomassa. Campinas - SP, Brazil: Galoá, 2015. http://dx.doi.org/10.17648/sinaferm-2015-34116.

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Rojas-Verde, G., M. M. Iracheta-Cárdenas, L. J. Galán-Wong, and K. Arévalo-Niño. "Production of amylases, CMCases, xylanases and ligninolytic enzymes by white-rot fungi in solid and liquid fermentation." In Proceedings of the III International Conference on Environmental, Industrial and Applied Microbiology (BioMicroWorld2009). WORLD SCIENTIFIC, 2010. http://dx.doi.org/10.1142/9789814322119_0122.

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Winarsa, Rudju, Ramdhan Putrasetya, Azizah, Farah Salma, Siswoyo, and Kahar Muzakhar. "Purification of an Extracellular Amylase Produced by <i>Aspergillus niger</i> ICP2 through Submerged Fermentation." In The 4th International Conference on Science and Technology Applications. Switzerland: Trans Tech Publications Ltd, 2023. http://dx.doi.org/10.4028/p-9253gj.

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The future applications of amylase have sparked the interest of several industries, resulting in the discovery of possible amylase-producing microbes. Aspergillus niger ICP2 was an indigenous fungus isolated from coffee pulp that shows amylolytic activity after growing on a soluble starch agar. In this study, we optimized the production and successfully purified the amylase from Aspergillus niger ICP2. Amylase optimization production was performed for a 7-day of incubation under submerged fermentation. The amylase activity was measured using the iodin method, and the total protein was quantified spectrophotometrically at 280 nm. Purifying amylase crude extract conducted such as ammonium sulfate precipitation, dialysis, and anion-exchange chromatography. Amylase was maximally precipitated at 90% saturation, followed by dialysis on a 10 kDa column, increasing specific activity up to 12.17 U/mg and purity multiples of 9.31 times. Two peaks of amylase activity were formed when the dialyzed amylase was loaded onto anion exchange chromatography with specific activities of 14.47 U/mg (fraction I) and 32.73 U/mg (fraction II). The increase in specific activity and purity fold indicated that the amylase purification process was successful.
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Muzakhar, Kahar, Ramdhan Putrasetya, Azizah, Farah Salma, Rudju Winarsa, and Siswoyo. "Characterization of Two Purified Amylase Produced from <i>Aspergillus niger</i> ICP2 and its Immobilization Using Activated Carbon." In The 4th International Conference on Science and Technology Applications. Switzerland: Trans Tech Publications Ltd, 2023. http://dx.doi.org/10.4028/p-s88747.

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Amylase is essential in the industrial sector, but there are some challenges with its low reusability efficiency. The catalytic activity of the amylase can be affected by using an activated carbon matrix as an immobilization technique. In this study, we characterized the purified amylase of Aspergillus niger ICP2 and immobilized it to activated carbon. Amylase production from A. niger ICP2 was performed throughout a 7-day incubation. After partial purification, two amylase fractions were generated, including 90% saturation ammonium sulfate precipitation, a 10-kDa hollow fiber dialysis column, and anion exchange chromatography. Thin-layer chromatography analysis showed the presence of glucose in fractions I and II, indicating glucoamylase activity. Both fractions had optimum pH and temperatures at 4.5 and 70°C, respectively. Fraction I was stable at acidic pH (3.5-5), while the stability of fraction II was in the range of acid to base (4-7.5) after incubation for 1 hour at 37°C. Both fractions displayed the same pattern of temperature stability (30-50°C) when incubated for 1 hour at optimum buffer. Activated carbon was used to immobilize amylase fraction II, which demonstrated the ability to hydrolysis the starch up to five times with a reduction in the activity of 50.4%. These results showed promising hydrolysis reusability by amylase immobilized using activated carbon.
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Keke, Anete, and Ingmars Cinkmanis. "α-amylase activity in freeze-dried and spray-dried honey." In Research for Rural Development 2020. Latvia University of Life Sciences and Technologies, 2020. http://dx.doi.org/10.22616/rrd.26.2020.017.

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Honey is a naturally supersaturated sugar solution, which tends to crystallize. The crystallization of honey can lead to unwanted fermentation that can have a negative impact to honey quality. The production of honey powder could be an alternative method to prevent honey from fermentation. Honey powder could be used as alternative substitute to liquid honey that would allow to use this product more widely in the food industry. α-amylase activity is one of the most important parameters to evaluate the quality of honey. The aim of this study was to investigate the effect of freeze-drying and spray-drying on honey α-amylase activity. Detection of α-amylase activity was carried out by spectrophotometric method. High-performance liquid chromatography was used to determine the content of hydroxymethylfurfural in the powders. The obtained results showed that both drying methods had a negative impact to the enzyme activity in the samples. The lowest activity of α-amylase (8.3 DN) was measured in the spray-dried honey powder. Concentration of hydroxymethylfurfural (HMF) in the powders did not exceed required concentration 40 mg kg-1.
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Guice, Justin, Caroline Best, Morgan Hollins, Kelly Tinker, and Sean Garvey. "Fungal Digestive Enzymes Promote Macronutrient Hydrolysis in the INFOGEST in vitro Simulation of Digestion." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/agsn3911.

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Fungal enzymes are common ingredients in dietary supplements that support digestion. At adequate concentrations, exogenous enzymes may improve digestion by hydrolyzing macronutrients beyond acid-mediated hydrolysis, endogenous gastric pepsin, and pancreatic enzymes alone. The purpose of this study was to test the hydrolytic efficacy of 6 commercial fungal enzymes—three proteases, a lipase, an amylase, and a glucoamylase—in the INFOGEST static in vitro simulation of gastrointestinal digestion. The efficacy of 5 doses of each enzyme was determined by measuring free amino nitrogen (FAN), glycerol, maltose, and glucose concentrations following salivary-gastric (SG) and full salivary-gastric-intestinal (SGI) simulations of digestion of an oral nutritional supplement. In the SG simulation, the 3 proteases, lipase, and combination of amylase and glucoamylase promoted greater hydrolysis of dietary protein, fat, and carbohydrates, respectively, compared to control conditions. Acid protease (Aspergillus niger) treatment increased FAN concentrations than controls from 27% at the lowest dose to 142% greater than controls at the highest dose (p<0.0001). Fungal protease (A. oryzae) treatment increased FAN concentration at the highest dose (160,000 HUT, p=0.0115). Peptidase (A. melleus) treatment promoted higher FAN concentrations, up to 50% increase at the highest dose (160 LAPU, p<0.0001). Glycerol concentrations increased across all lipase treatments (p<0.0001), from 4.1-fold to 11.2-fold increases at the lowest and highest doses, respectively. All doses of amylase increased glucose concentrations (p<0.0001), and maltose concentrations started increasing at 4,000 SKB units (p=0.0010). In the SGI simulation, FAN concentrations following protease treatments were similar to control, suggesting little benefit beyond pancreatin alone in this static simulation of healthy digestion. Lipase and amylase/glucoamylase treatments, however, did increase glycerol (p<0.0001) and maltose/glucose concentrations (p<0.0001), respectively, compared to controls in the full SGI simulation. These data demonstrate that exogenous, fungal enzymes can improve macronutrient digestion under the acidic conditions of the gastric simulation, as well as the intestinal simulation.
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Primožič, Mateja, Željko Knez, and Maja Leitgeb. "Activity of α--Amylase from P. ostreatus Grown on Waste Substrates." In International Conference on Technologies & Business Models for Circular Economy. University of Maribor Press, 2022. http://dx.doi.org/10.18690/um.fkkt.2.2022.7.

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Forest and agricultural waste can be a major development and ecological opportunity. Therefore, it is reasonable to use biological waste further to produce energy and for the manufacture of certain products with high added value, such as, for example, the cultivation of fungi and, consequently, the production of biocatalysts with high market value. In addition, the use of agriculture waste for Oyster mushroom (Pleurotus ostreatus) growth can be integrated to waste management and the development of the bioeconomy. The cultivation of P. ostreatus using waste plant biomass from agriculture (straw, grass, courgettes, cucumbers, peaches, apricots, pears, and peppers) was performed in order to obtain the highest increase in biomass production of the cultivated mushroom and as a potential source of α-amylase, with high catalytic activity. The highest α-amylase activities were achieved when pears or apricots were used as a substrate for P. ostreatus cultivation.
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Dieguez-Santana, Karel, and Bakhtiyor Rasulev. "Machine Learning Analysis of α-amylase Inhibitors." In MOL2NET'21, Conference on Molecular, Biomedical & Computational Sciences and Engineering, 7th ed. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/mol2net-07-11229.

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Mohamed, Mai, and Patricia Kruk. "Abstract 5080: Amylase overexpression promotes ovarian cancer invasion." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-5080.

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Reports on the topic "Amylases"

1

Mulrine, Brandon L., Michael F. Sheehan, Lolita M. Burrell, and Michael D. Matthews. Measuring Stress and Ability to Recover from Stress with Salivary Alpha-Amylase Levels. Fort Belvoir, VA: Defense Technical Information Center, April 2011. http://dx.doi.org/10.21236/ada540975.

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Karcheva-Bahchevanska, Diana, Paolina Lukova, Mariana Nikolova, Rumen Mladenov, and Iliya Iliev. Inhibition Effect of Bulgarian Lingonberry (Vaccinium vitis-idaea L.) Extracts on α‒Amylase Activity. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, February 2019. http://dx.doi.org/10.7546/crabs.2019.02.10.

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Harmon, David L., Israel Bruckental, Gerald B. Huntington, Yoav Aharoni, and Amichai Arieli. Influence of Small Intestinal Protein on Carbohydrate Assimilation in Beef and Dairy Cattle. United States Department of Agriculture, August 1995. http://dx.doi.org/10.32747/1995.7570572.bard.

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The long term goal of the proposed research, "Influence of small intestinal protein on carbohydrate assimilation and metabolism in beef and dairy cattle" was to define the limits of small intestinal starch digestion and clarify regulatory mechanisms involved in starch assimilation in cattle. It was hypothesized that dietary protein plays a critical role in the regulation of intestinal digestion; however, studies clearly identifying this role were lacking. The first two experiments quantified starch digestion (disappearance from the small intestine) in response to known increments in duodenal protein supply and found that the quantity of DM, OM and starch disappearing from the small intestine increased linearly (P <.01) with protein infusion. A follow-up experiment also demonstrated that casein infusion linearly increased pancreatic a-amylase concentration and secretion rate. The final experiment provided critical data on metabolic fates of glucose derived from intestinal starch digestion. These data demonstrated that increasing postruminal starch supply does increase the metabolism of glucose by visceral tissues: however, this increase is minor (20%) compared with the increase in portal production (70%). These changes can have a dramatic impact on the glucose economy of the animal and result in large increases in the amount of glucose reaching peripheral tissues.
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