Journal articles: 'Fungal amylase'

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Khushk, Imrana. "Environmental Friendly Production of Amylase from Aspergillus niger EFRL-FC-024 Using Corn Waste as Carbon Source." Pakistan Journal of Analytical & Environmental Chemistry 22, no. 1 (June 23, 2021): 165–71. http://dx.doi.org/10.21743/pjaec/2021.06.17.

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Amylase is an indispensable and industrially important enzyme that hydrolyzes carbohydrates particularly starch into simple sugars. Amylase enzymes have been isolated from various sources such as microbes, animals and plants. However, microorganisms are highly preferred as compared to plants and animal sources. Amylases of fungal origin are highly stable compared to amylases produced by bacterial species. The aim of this study was to investigate the production of extracellular amylase enzyme from Aspergillus niger EFRL-FC-024 using sugarcane bagasse and corn waste as an energy source under submerge fermentation conditions. Primarily, the fungal strain was grown for 6 days using sugarcane bagasse and corn waste, respectively. Mainly, the growth of a microorganism was also evaluated using different pH, temperature and incubation periods. The results revealed maximum amylase production of 1.64 U/mL when A. niger was cultured for 96 h using corn waste. Moreover, addition of different nitrogen sources showed the highest amylase production when peptone was supplemented as a nitrogen source. Finally, the effect of pH indicated maximal concentration of amylase enzyme at pH 6.0. The present study will highly be beneficial to explore the role of fungal strain A. niger in amylase production at Industrial levels.

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Singh, Shalini, Sanamdeep Singh, Vrinda Bali, Lovleen Sharma, and Jyoti Mangla. "Production of Fungal Amylases Using Cheap, Readily Available Agriresidues, for Potential Application in Textile Industry." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/215748.

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The study aimed at isolation and screening of fungal amylase producer, optimization of solid state fermentation conditions for maximum amylase production by the best amylase producer, and characterization of the crude amylases, so produced.Aspergillus fumigatusNTCC1222 showed the highest amylase activity (164.1 U/mL) in secondary screening under SSF conditions and was selected for further studies. The test strain showed maximum amylase production (341.7 U/mL) and supernatant protein concentration (9.7 mg/mL) for incubation period (6 days), temperature (35°C), initial pH (6.0), nutrient salt solution as moistening agent, and beef extract as nitrogen source. Pomegranate peel produced maximum amylase activity, but wheat bran (only slightly lesser amylase activity as compared to that of pomegranate peel) was chosen for further studies, keeping in mind the seasonal availability of pomegranate peel. TLC confirmed the amylase produced to beα-type and 60 kDa was the molecular weight of the partially purified amylase. The enzyme showed maximum enzyme activity at pH 6.0, temperature of 55°C, and incubation time of 60 minutes. UV (616.0 U/mL) and chemical (814.2 U/mL) mutation enhanced amylase activity as compared to wild test strain. The study indicates thatAspergillus fumigatusNTCC1222 can be an important source of amylase and the crude enzyme, hence obtained, can be cost effectively applied in multiple sections of textile wet processing.

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Okunwaye, T., P. O. Uadia, B. O. Okogbenin, E. A. Okogbenin, D. C. Onyia, and J. U. Obibuzor. "Amylase-Producing Fungi and Bacteria Associated with Some Food Processing Wastes." Nigerian Journal of Biotechnology 38, no. 1 (July 27, 2021): 74–82. http://dx.doi.org/10.4314/njb.v38i1.9.

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Amylases are enzymes that catalyze the hydrolysis of glycosidic bonds present in starch to release simple sugars. They are one of the most important enzymes in numerous commercial processes. In this investigation, fungal and bacterial strains from the following agro-industrial wastes were isolated and screened for amylolytic ability: soil from oil palm plantation, shea seed, date fruit, coconut meat, cassava effluent, cassava peel, cassava tubers, yam and potato tubers, starch medium, parboiled water from noodles and rice. The results revealed the presence of Geotrichum, Aspergillus, Penicillium, Trichoderma, Rhizopus and Fusarium spp. Five major genera of bacterial species namely Corynebacterium, Pseudomonas, Lactobacillus, Micrococcus and Bacillus were isolated and screened for amylase activity. Cassava soil had the highest heterotrophic bacterial count of 5.7 x105cfu/g and coconut meat waste had the lowest heterotrophic bacterial count of 1.3 x105cfu/g. All isolated microorganisms had the amylolytic ability. The fungal isolates had higher amylase activity when compared with the bacterial isolates. This investigation reveals organisms with high amylase activity.

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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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Fakhoury, A. M., and C. P. Woloshuk. "Inhibition of Growth of Aspergillus flavus and Fungal α-Amylases by a Lectin-Like Protein from Lablab purpureus." Molecular Plant-Microbe Interactions® 14, no. 8 (August 2001): 955–61. http://dx.doi.org/10.1094/mpmi.2001.14.8.955.

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Aspergillus flavus is a fungal pathogen of maize causing an important ear rot disease when plants are exposed to drought and heat stress. Associated with the disease is the production of aflatoxins, which are a series of structurally related mycotoxins known to be carcinogenic. Previous research has suggested that the α-amylase of A. flavus promotes aflatoxin production in the endosperm of infected maize kernels. We report here the isolation and characterization of a 36-kDa α-amylase inhibitor from Lablab purpureus (AILP). AILP inhibited the α-amylases from several fungi but had little effect on those from animal and plant sources. The protein inhibited conidial germination and hyphal growth of A. flavus. The amino acid sequence indicated that AILP is similar to lectin members of a lectin-arcelin-α-amylase inhibitor family described in common bean and shown to be a component of plant resistance to insect pests. AILP also agglutinated papain-treated red blood cells from human and rabbit. These data indicate that AILP represents a novel variant in the lectin-arcelin-α-amylase inhibitor family of proteins having lectin-like and α-amylase inhibitory activity.

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Chen, Z. Y., R. L. Brown, J. S. Russin, A. R. Lax, and T. E. Cleveland. "A Corn Trypsin Inhibitor with Antifungal Activity Inhibits Aspergillus flavus α-Amylase." Phytopathology® 89, no. 10 (October 1999): 902–7. http://dx.doi.org/10.1094/phyto.1999.89.10.902.

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In this study, we found that the inhibition of fungal growth in potato dextrose broth (PDB) medium by the 14-kDa corn trypsin inhibitor (TI) protein, previously found to be associated with host resistance to aflatoxin production and active against various fungi, was relieved when exogenous α-amylase was added along with TI. No inhibitory effect of TI on fungal growth was observed when Aspergillus flavus was grown on a medium containing either 5% glucose or 1% gelatin as a carbon source. Further investigation found that TI not only inhibited fungal production of extracellular α-amylase when A. flavus was grown in PDB medium containing TI at 100 μg ml-1 but also reduced the enzymatic activity of A. flavus α-amylase by 27%. At a higher concentration, however, TI stimulated the production of α-amylase. The effect of TI on the production of amyloglucosidase, another enzyme involved in starch metabolism by the fungus, was quite different. It stimulated the production of this enzyme during the first 10 h at all concentrations studied. These studies suggest that the resistance of certain corn genotypes to A. flavus infection may be partially due to the ability of TI to reduce the production of extracellular fungal α-amylase and its activity, thereby limiting the availability of simple sugars for fungal growth. However, further investigation of the relationship between TI levels and fungal α-amylase expression in vivo is needed.

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Słomińska, Lucyna, Roman Zielonka, and Leszek Jarosławski. "The unconventional single stage hydrolysis of potato starch." Polish Journal of Chemical Technology 15, no. 3 (September 1, 2013): 7–14. http://dx.doi.org/10.2478/pjct-2013-0037.

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Abstract Enzymatic depolymerisation of starch to glucose or maltose is carried out by starch- degrading amylases during a two-stage hydrolysis: liquefaction using bacterial α-amylase followed by saccharification with glucogenic (fungal amylase) or maltogenic (fungal or bacterial) amylases. As a rule, these enzymes are applied separately, following the recommendations concerning their action provided by the enzyme manufacturers. The study presents our attempts to determine the reaction conditions for a simultaneous action of liquefying and saccharifying enzymes on pre-treated potato starch. Hydrolysis was run by Liquozyme Supra, Maltogenase 4000L and San Super 360L enzymes (Novozymes) at different temperatures. During the single-stage method of starch hydrolysate production the most desirable results was obtained for the maltose hydrolysate at 80°C (51.6 DE) and for the glucose hydrolysate at 60°C (96 DE). The analyses indicate that the application of a single-stage hydrolysis of starch to maltose or glucose makes it possible to obtain a degree of starch saccharification comparable with that obtained in the traditional two-stage hydrolysis.

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8

Sariozlu, N. Yilmaz, and R. Demirel. "Screening of fungal strains for amylase production." New Biotechnology 25 (September 2009): S73. http://dx.doi.org/10.1016/j.nbt.2009.06.318.

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9

Arakawa, Tsutomu, Lynne Hung, and Linda O. Narhi. "Stability of fungal ?-amylase in sodium dodecylsulfate." Journal of Protein Chemistry 11, no. 2 (April 1992): 111–17. http://dx.doi.org/10.1007/bf01025216.

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10

Essiedu, Justice Amakye, Frank Seth Johnson, and Francis Ayimbila. "ISOLATION OF AMYLASE PRODUCING FUNGI FROM CASSAVA FLOUR." Fungal Territory 4, no. 1 (March 17, 2021): 5–9. http://dx.doi.org/10.36547/ft.151.

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Amylases are among the most important enzymes with potential applications in the present-day industry. Thus, isolating pure culture from cassava as the cheap source has manifold importance for food industries. In the present study, eleven amylase producing fungal strains were isolated from cassava flour and growth pattern, as well as optimum growth condition, was determined. All isolates showed amylases activity but isolate BR005, BR001 and GR003 recorded maximum clear zone diameters of 54.75 ± 0.957 mm, 53.25 ±0.645 mm 51.5 ± 1.414 mm, respectively. The submerged fermentation method was employed for crude amylase and biomass production. There were significant differences (p˂0.05) in starch concentrations and growth rates between the three isolates. GR003 and BR005 attained their optimal amylase activities of 4.23±0.25 U/mL and 3.75±3.16 U/mL at 50 °C, respectively, whiles BR001 attained its optimum amylase activity of 3.43±0.77 at 60 °C. Whereas, BR005, BR001 and GR003 attained their optimal amylase activity of 5.14±1.99 U/mL, 4.53±0.01 U/mL and 1.25±1.11 U/mL at a pH range of 6 to 7, making them neutrophilic fungi. Moreover, isolates BR005, BR001 and GR003 recorded the highest amylase activities of 4.31±0.14U/mL, 4.67±1.16±U/mL and 3.16±0.12U/mL at the starch concentrations of 3%, 2%, and 2.5% and fermentation period of 48 h, 66 h and 42 h, respectively. Lastly, BR005, BR001 and GR003 achieved their optimal amylase activities of 5.41±0.11U/mL, 6.24±0.14 U/mL and 6.22±0.12 U/mL at 48 h, 66 h and 42 h of incubation, accordingly. Indicating that cassava flour is a good source of amylolytic fungi with a potential application under wide conditions.

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11

Grewal, Ravneet K., Baldeep Kaur, and Gagandeep Kaur. "Kinetic Behaviour of Amylase According to pH: A New Perspective for Starch Hydrolysis Process." Current Enzyme Inhibition 16, no. 2 (June 30, 2020): 135–44. http://dx.doi.org/10.2174/1573408016666200316114808.

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Background: Amylases are the most widely used biocatalysts in starch saccharification and detergent industries. However, commercially available amylases have few limitations viz. limited activity at low or high pH and Ca2+ dependency. Objective: The quest for exploiting amylase for diverse applications to improve the industrial processes in terms of efficiency and feasibility led us to investigate the kinetics of amylase in the presence of metal ions as a function of pH. Methods: The crude extract from soil fungal isolate cultures is subjected to salt precipitation, dialysis and DEAE cellulose chromatography followed by amylase extraction and is incubated with divalent metal ions (i.e., Ca2+, Fe2+, Cu2+, and Hg2+); Michaelis-Menton constant (Km), and maximum reaction velocity (Vmax) are calculated by plotting the activity data obtained in the absence and presence of ions, as a function of substrate concentration in Lineweaver-Burk Plot. Results: Kinetic studies reveal that amylase is inhibited un-competitively at 5mM Cu2+ at pH 4.5 and 7.5, but non-competitively at pH 9.5. Non-competitive inhibition of amylase catalyzed starch hydrolysis is observed with 5mM Hg2+ at pH 9.5, which changes to mixed inhibition at pH 4.5 and 7.5. At pH 4.5, Ca2+ induces K- and V-type activation of amylase catalyzed starch hydrolysis; however, the enzyme has V-type activation at 7mM Ca2+ under alkaline conditions. Also, K- and V-type of activation of amylase is observed in the presence of 7mM Fe2+ at pH 4.5 and 9.5. Conclusion: These findings suggest that divalent ions modulation of amylase is pH dependent. Furthermore, a time-saving and cost-effective solution is proposed to overcome the challenges of the existing methodology of starch hydrolysis in starch and detergent industries.

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12

Ahmad, M. A., U. Isah, I. A. Raubilu, S. I. Muhammad, and D. Ibrahim. "An overview of the enzyme: Amylase and its industrial potentials." Bayero Journal of Pure and Applied Sciences 12, no. 1 (April 15, 2020): 352–58. http://dx.doi.org/10.4314/bajopas.v12i1.53s.

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Amylases are group of enzymes produced by plants, animals and microorganisms, the enzyme has the ability to hydrolyze or degrade starch molecules into polymers containing units of glucose, thus, it is one of the most useful enzymes used by industries dependent on starch in their production processes. The enzyme has varying applications in food, fermentation, textile, pharmaceutical industries among others. Generally, amylase from microbial sources (i.e. fungal and bacterial origin) has over shadowed others in industrial usage. As such, this Paper aimed at reviewing amylase enzyme as a whole and some of its common industrial applications. The review visited the types of amylase based on hydrolases classification, its sources with emphasis to microorganisms, methods of production as well as effects of some chemical and physical parameters. The review also discusses some of the most common industrial application or uses of amylase enzyme in food, brewing, chemicals, paper, pharmaceutical, textile industries to mention but few. In conclusion, the reviewers suggest the use of microbial amylase due to it easy and simple technique in production, lower capital investment, lower energy requirement and high yield during production, exploration of more microbes with enzyme production potentials as well as improved industrial Scale production of the amylase for the betterment of the economy and improved industrial production of products. Key: Amylase, Application, Enzyme, Industry, Microbes and Starch.

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13

Ali, F. S., and A. A. Abdel-Moneim. "Effect of chemicals on fungal α-amylase activity." Zentralblatt für Mikrobiologie 144, no. 8 (1989): 623–28. http://dx.doi.org/10.1016/s0232-4393(89)80126-x.

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14

Cauvain, Stanley P., and Norman Chamberlain. "The bread improving effect of fungal α-amylase." Journal of Cereal Science 8, no. 3 (November 1988): 239–48. http://dx.doi.org/10.1016/s0733-5210(88)80035-3.

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15

TSUJISAKA, Yoshio. "Remembrance of the study on fungal saccharogenic amylase." Journal of the Japanese Society of Starch Science 34, no. 2 (1987): 137–39. http://dx.doi.org/10.5458/jag1972.34.137.

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Sander, Raulf-Heimsoth, Van Kampen, and Baur. "Is fungal α-amylase in bread an allergen?" Clinical & Experimental Allergy 30, no. 4 (April 2000): 560–65. http://dx.doi.org/10.1046/j.1365-2222.2000.00746.x.

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17

Graber, M., and D. Combes. "Effect of polyols on fungal alpha-amylase thermostability." Enzyme and Microbial Technology 11, no. 10 (October 1989): 673–77. http://dx.doi.org/10.1016/0141-0229(89)90007-0.

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18

Figueira, Edson L. Z., Elisa Y. Hirooka, Elizabeth Mendiola-Olaya, and Alejandro Blanco-Labra. "Characterization of a Hydrophobic Amylase Inhibitor from Corn (Zea mays) Seeds with Activity Against Amylase from Fusarium verticillioides." Phytopathology® 93, no. 8 (August 2003): 917–22. http://dx.doi.org/10.1094/phyto.2003.93.8.917.

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A hydrophobic 19.7-kDa amylase inhibitor (AI) was purified from corn kernels by 95% ethanol extraction and anionic exchange chromatography. The AI has an isoelectric point of 3.6 and was very stable at different pH values and high temperatures, maintaining 47.6% activity after heating to 94°C for 60 min. Amino acid analysis indicated high valine, leucine, glycine, alanine, and glutamic acid/glutamine content, and especially high valine content (41.2 mol%). This inhibitor is not a glycoprotein. It required 30-min preincubation to maximize complex enzyme-inhibitor formation when the amylase from Fusarium verticillioides was tested. The optimal pH of interaction was 6.5. It showed broad-spectrum activity including the following amylases: human saliva, porcine pancreas, F. verticillioides, as well as those from some insects of agricultural importance (Acanthoscelides obtectus, Zabrotes subfasciatus, Sitophilus zeamais, and Prostephanus truncatus). This novel hydrophobic protein not only inhibited the amylase from F. verticillioides but also decreased the conidia germination. Thus, this protein represents an approach to decrease the production of fumonisin in corn, either by using it as a molecular marker to detect fungal resistance or through genetic engineering.

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Smith, T. A., K. P. S. Lumley, and E. H. K. Hui. "Allergy to flour and fungal amylase in bakery workers." Occupational Medicine 47, no. 1 (1997): 21–24. http://dx.doi.org/10.1093/occmed/47.1.21.

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20

Ire, Francis, Sotonye Ipalibo Wokoma, and Augustine Okoli. "Isolation, Screening and Time Course Study of Amylase-producing Fungi from Garri Processing Environment." Journal of Life and Bio Sciences Research 1, no. 3 (December 14, 2020): 68–75. http://dx.doi.org/10.38094/jlbsr1325.

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Amylases (E.C.3.2.1.1) are enzymes which catalyze the breakdown of -1,4 glycosidic linkages of starch to simple sugars and different monomeric products. Microbial amylases are essential enzymes compared with animals and plants amylases in industrial applications. Thus, in southern Nigeria, garri processing waste-water from mills poses a serious environmental challenge and this situation could be exploited by utilizing microorganisms colonizing the area to manufacture microbial products. This present study was aimed at evaluating the potential of fungi isolated from garri processing environment for amylase secretion and conduct a time course study of the enzyme production. Fungi were isolated from the soil and waste water from garri processing sites using Standard Microbiological Procedures. The five fungi isolated from garri processing environmental samples were screened using Lugols iodine. Three fungal isolates were then selected on the hydrolysis of starch in qualitative zonation agar plates but one isolate named B among them was better in starch hydrolysis related to highest clear zone plates. After qualitative screening, the three hyper production amylase extracted fungi were identified according to the morphological characteristics. The hyper producing amylase isolate B was then identified as Aspergillus flavus (RCBBR_AEAFUN2) and recorded as a novel strain in southern Nigeria according to molecular characteristics, which was selected for further studies. The current results of time course study showed that the maximum growth (2.453 g) occurred after 24 h of incubation at pH 4.5 while maximum enzyme production (2.3 U/ml/min) was obtained after 96 h of incubation at pH 3.5. Therefore, the hyper producing amylase from garri processing sites, Aspergillus flavus (RCBBR_AEAFUN2) novel strain has great prospects for future biotechnological and industrial applications and help in ameliorating the environmental pollution posed by the waste-water.

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van der Kaaij, R. M., X. L. Yuan, A. Franken, A. F. J. Ram, P. J. Punt, M. J. E. C. van der Maarel, and L. Dijkhuizen. "Two Novel, Putatively Cell Wall-Associated and Glycosylphosphatidylinositol-Anchored α-Glucanotransferase Enzymes of Aspergillus niger." Eukaryotic Cell 6, no. 7 (May 11, 2007): 1178–88. http://dx.doi.org/10.1128/ec.00354-06.

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ABSTRACT In the genome sequence of Aspergillus niger CBS 513.88, three genes were identified with high similarity to fungal α-amylases. The protein sequences derived from these genes were different in two ways from all described fungal α-amylases: they were predicted to be glycosylphosphatidylinositol anchored, and some highly conserved amino acids of enzymes in the α-amylase family were absent. We expressed two of these enzymes in a suitable A. niger strain and characterized the purified proteins. Both enzymes showed transglycosylation activity on donor substrates with α-(1,4)-glycosidic bonds and at least five anhydroglucose units. The enzymes, designated AgtA and AgtB, produced new α-(1,4)-glycosidic bonds and therefore belong to the group of the 4-α-glucanotransferases (EC 2.4.1.25). Their reaction products reached a degree of polymerization of at least 30. Maltose and larger maltooligosaccharides were the most efficient acceptor substrates, although AgtA also used small nigerooligosaccharides containing α-(1,3)-glycosidic bonds as acceptor substrate. An agtA knockout of A. niger showed an increased susceptibility towards the cell wall-disrupting compound calcofluor white, indicating a cell wall integrity defect in this strain. Homologues of AgtA and AgtB are present in other fungal species with α-glucans in their cell walls, but not in yeast species lacking cell wall α-glucan. Possible roles for these enzymes in the synthesis and/or maintenance of the fungal cell wall are discussed.

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Sinha, Durgeshnandani, Trilochan Satapathy, Parag Jain, Jhakeshwar Prasad Chandel, Divya Sahu, Bhavna Sahu, Abhishek Verma, Shalini Singh, Khushboo Verma, and Rahul Rathore. "In Vitro Antidiabetic Effect of Neohesperidin." Journal of Drug Delivery and Therapeutics 9, no. 6 (November 15, 2019): 102–9. http://dx.doi.org/10.22270/jddt.v9i6.3633.

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Objective: The present study was performed to determine in vitro antidiabetic effect of neohesperidin. To evaluate inhibitory effect of neohesperidin on α-amylase and α-glucosidase diabetes causing enzyme. Methods and Materials: Invitro carbohydrate metabolizing enzyme based inhibitory methods were used to determine antidiabetic effect of neohesperidin. Alpha (α)-amylase inhibitory assay was performed using different sources i.e. wheat alpha (α)-amylase enzyme, salivary alpha (α)-amylase and fungal alpha (α)-amylase assay. Alpha (α)-glucosidase inhibitory assay was performed using alpha (α)-glucosidase (B. stearothermophil), alpha (α)-glucosidase rat intestine and alpha (α)-glucosidase from baker’s yeast. Sucrase inhibitory assay from rat small intestine. Result: Neohesperidin possess a potent anti-diabetic by significantly inhibiting alpha amylase activity. Conclusion: It was concluded that enzyme inhibitory activity of neohesperidin shown a significantly higher inhibitory activity on alpha-amylase in comparision to alpha-glucosidase & Sucrase enzymes. Keywords: Neohespiridin, acarbose, alpha-amylase, alpha-glucosidase

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Pavan Kumar Kurakula, Tharun D, Mahantesh S, Krishna O, Sudheer A, Mujahid SM, and Sai vikas S. "Evaluation of in-vitro antidiabetic activity of leaf juice of Plectranthus amboinicus (lour.)." International Journal of Novel Trends in Pharmaceutical Sciences 10, no. 1 (June 17, 2020): 9–17. http://dx.doi.org/10.26452/ijntps.v10i1.1143.

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Diabetes mellitus ‘the disease of modern civilization’ is characterized by chronic hyperglycaemia. The management of elevated post prandial glucose is critical to control the sequale of complications and α-amylase, α-glucosidases are responsible for elevated plasma glucose. Enzyme inhibitors in current clinical practice like acarbose, voglibose etc. are known to cause various gastrointestinal side effects. The present study was aimed to screen for potential α-amylase and α-glucosidase inhibitors from natural sources by in–vitro antidiabetic assays to overcome the side effects and toxicity. Different concentrations of leaf juice of Plectranthus amboinicus Lour. (20, 40, 60, 80 &100 μg/ml) were tested against fungal α-amylase and α-glucosidases isolated from albino rat small intestine and a prominent dose dependent inhibition of the enzymes was observed comparable with the marketed product, Acarbose. The IC50 values of LJPA and acarbose on fungal α-amylase was found to be 83.15 &52.15 μg/ml respectively. The IC50 values of LJPA and acarbose on α-glucosidase was found to be 92.44 &54.84 μg/ml respectively. The protein concentration of leaf juice was found to be 10.6 mg/ml.

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Banu, I., G. Stoenescu, V. Ionescu, and I. Aprodu. "Estimation of the baking quality of wheat flours based on rheological parameters of the mixolab curve." Czech Journal of Food Sciences 29, No. 1 (February 14, 2011): 35–44. http://dx.doi.org/10.17221/40/2009-cjfs.

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The Mixolab device in view of the characterisation of the thermo-mechanical behaviour of ten different flours, and establishing the correlations between the rheological parameters of wheat flour supplemented with different additives such as fungal α-amylase, fungal hemicellulase, and fungal xylanase weres exploted. The rheological measurements were performed using the Mixolab, Alveograph, and Rheofermentometer. Our results indicated significant positive and negative correlations between the parameters investigated. The changes of the Mixolab curve trend depended on the amylase doses. Significant correlations were established also between the Mixolab parameters and the results of the baking tests; the β slope, C2, C3, and C4 were positively correlated with the specific volume of the bread. Taking into account the results obtained, we may conclude that Mixolab is a complex device that renders the evolution of the bread during the entire technological process, from the dough making to the starch retrogradation.

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Janíčková, Zuzana, and Štefan Janeček. "In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites." Molecules 26, no. 18 (September 21, 2021): 5704. http://dx.doi.org/10.3390/molecules26185704.

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This study brings a detailed bioinformatics analysis of fungal and chloride-dependent α-amylases from the family GH13. Overall, 268 α-amylase sequences were retrieved from subfamilies GH13_1 (39 sequences), GH13_5 (35 sequences), GH13_15 (28 sequences), GH13_24 (23 sequences), GH13_32 (140 sequences) and GH13_42 (3 sequences). Eight conserved sequence regions (CSRs) characteristic for the family GH13 were identified in all sequences and respective sequence logos were analysed in an effort to identify unique sequence features of each subfamily. The main emphasis was given on the subfamily GH13_32 since it contains both fungal α-amylases and their bacterial chloride-activated counterparts. In addition to in silico analysis focused on eventual ability to bind the chloride anion, the property typical mainly for animal α-amylases from subfamilies GH13_15 and GH13_24, attention has been paid also to the potential presence of the so-called secondary surface-binding sites (SBSs) identified in complexed crystal structures of some particular α-amylases from the studied subfamilies. As template enzymes with already experimentally determined SBSs, the α-amylases from Aspergillus niger (GH13_1), Bacillus halmapalus, Bacillus paralicheniformis and Halothermothrix orenii (all from GH13_5) and Homo sapiens (saliva; GH13_24) were used. Evolutionary relationships between GH13 fungal and chloride-dependent α-amylases were demonstrated by two evolutionary trees—one based on the alignment of the segment of sequences spanning almost the entire catalytic TIM-barrel domain and the other one based on the alignment of eight extracted CSRs. Although both trees demonstrated similar results in terms of a closer evolutionary relatedness of subfamilies GH13_1 with GH13_42 including in a wider sense also the subfamily GH13_5 as well as for subfamilies GH13_32, GH13_15 and GH13_24, some subtle differences in clustering of particular α-amylases may nevertheless be observed.

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Pritchard, Peter E. "Studies on the bread-improving mechanism of fungal alpha-amylase." Journal of Biological Education 26, no. 1 (March 1992): 12–18. http://dx.doi.org/10.1080/00219266.1992.9655237.

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Damián-Almazo, Juanita Yazmin, Alina Moreno, Agustin López-Munguía, Xavier Soberón, Fernando González-Muñoz, and Gloria Saab-Rincón. "Enhancement of the Alcoholytic Activity of α-Amylase AmyA from Thermotoga maritima MSB8 (DSM 3109) by Site-Directed Mutagenesis." Applied and Environmental Microbiology 74, no. 16 (June 13, 2008): 5168–77. http://dx.doi.org/10.1128/aem.00121-08.

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ABSTRACT AmyA, an α-amylase from the hyperthermophilic bacterium Thermotoga maritima, is able to hydrolyze internal α-1,4-glycosidic bonds in various α-glucans at 85°C as the optimal temperature. Like other glycoside hydrolases, AmyA also catalyzes transglycosylation reactions, particularly when oligosaccharides are used as substrates. It was found that when methanol or butanol was used as the nucleophile instead of water, AmyA was able to catalyze alcoholysis reactions. This capability has been evaluated in the past for some α-amylases, with the finding that only the saccharifying fungal amylases from Aspergillus niger and from Aspergillus oryzae present measurable alcoholysis activity (R. I. Santamaria, G. Del Rio, G. Saab, M. E. Rodriguez, X. Soberon, and A. Lopez, FEBS Lett. 452:346-350, 1999). In the present work, we found that AmyA generates larger quantities of alkyl glycosides than any amylase reported so far. In order to increase the alcoholytic activity observed in AmyA, several residues were identified and mutated based on previous analogous positions in amylases, defining the polarity and geometry of the active site. Replacement of residue His222 by glutamine generated an increase in the alkyl glucoside yield as a consequence of a higher alcoholysis/hydrolysis ratio. The same change in specificity was observed for the mutants H222E and H222D, but instability of these mutants toward alcohols decreased the yield of alkyl glucoside.

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Napitupulu, Toga Pangihotan, Nathaniel Reinhart Silaban, Atit Kanti, and I. Made Sudiana. "The effect of substrate composition on the activity of amylase and cellulase by Trichoderma harzianum strains under solid state fermentation." Journal of Microbial Systematics and Biotechnology 1, no. 2 (December 30, 2019): 41–48. http://dx.doi.org/10.37604/jmsb.v1i2.26.

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Trichoderma harzianum is a filamentous fungus that has been known to have biocontrol and plant growth-promoting ability. However, the propagation of this fungus particularly through solid state fermentation (SSF) and characterization of its enzyme activity as one the indicator of quality of fermentation process are still needed to be explored further. Rice grain and its derivative products have economically as well as nutrient composition features beneficial as substrates of fungal propagation through SSF. Therefore, the aim of this study was to investigate the effect of white rice, rice bran, and combination of white rice and rice bran on the activity of amylase and cellulase by Trichoderma harzianum strains under SSF. Two strains of the fungus, InaCC F116 and InaCC F89, as well as their consortium were employed as fungal inoculants. After closed fermentation in dark chamber at 30 ± 1°C for 7 days, the activity of amylolytic as well as cellulolytic enzyme was assayed. The result showed that the presence of rice bran as a substrate increased the activity of crude amylase and crude cellulase. In all substrates, the strain F116 has low activity of both enzymes. The fungal consortium improves the activity of crude enzymes in all substrates. Therefore, the amylase and cellulase activity by T. harzianum in SSF condition were strain- as well as substrate-dependent.

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McCleary, Barry V., Marian McNally, Dympna Monaghan, David C. Mugford, C. Black, R. Broadbent, M. Chin, et al. "Measurement of α-Amylase Activity in White Wheat Flour, Milled Malt, and Microbial Enzyme Preparations, Using the Ceralpha Assay: Collaborative Study." Journal of AOAC INTERNATIONAL 85, no. 5 (September 1, 2002): 1096–102. http://dx.doi.org/10.1093/jaoac/85.5.1096.

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Abstract This study was conducted to evaluate the method performance of a rapid procedure for the measurement of α-amylase activity in flours and microbial enzyme preparations. Samples were milled (if necessary) to pass a 0.5 mm sieve and then extracted with a buffer/salt solution, and the extracts were clarified and diluted. Aliquots of diluted extract (containing α-amylase) were incubated with substrate mixture under defined conditions of pH, temperature, and time. The substrate used was nonreducing end-blocked p-nitrophenyl maltoheptaoside (BPNPG7) in the presence of excess quantities of thermostable α-glucosidase. The blocking group in BPNPG7 prevents hydrolysis of this substrate by exo-acting enzymes such as amyloglucosidase, α-glucosidase, and β-amylase. When the substrate is cleaved by endo-acting α-amylase, the nitrophenyl oligosaccharide is immediately and completely hydrolyzed to p-nitrophenol and free glucose by the excess quantities of α-glucosidase present in the substrate mixture. The reaction is terminated, and the phenolate color developed by the addition of an alkaline solution is measured at 400 nm. Amylase activity is expressed in terms of Ceralpha units; 1 unit is defined as the amount of enzyme required to release 1 μmol p-nitrophenyl (in the presence of excess quantities of α-glucosidase) in 1 min at 40°C. In the present study, 15 laboratories analyzed 16 samples as blind duplicates. The analyzed samples were white wheat flour, white wheat flour to which fungal α-amylase had been added, milled malt, and fungal and bacterial enzyme preparations. Repeatability relative standard deviations ranged from 1.4 to 14.4%, and reproducibility relative standard deviations ranged from 5.0 to 16.7%.

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MD Makut, FU Alfa, IK Ekeleme, JE Owuna, and NJ Emelogu. "Production of amylases by some aspergillus and fusarium species isolated from waste corncobs in Keffi, Nigeria." GSC Biological and Pharmaceutical Sciences 16, no. 2 (August 30, 2021): 122–29. http://dx.doi.org/10.30574/gscbps.2021.16.2.0216.

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Amylases are important industrial enzymes that have wide applications ranging from conversion of starch to sugar syrups, to the production of cyclodextrins for the pharmaceutical industry. This investigation aimed at production of amylases using Aspergillus and Fusarium species isolated from waste-corncobs in Keffi Nigeria. Standard microbiological methods were employed for isolation and identification of the fungal isolates. The yields of amylases produced by fungi isolates were determined using Spectrometry. The isolation rate of Aspergillus and Fusarium species was high in location A, C and D with 60% and location B with 40%. The percentage occurrence of the isolates demonstrated that Aspergillus carneus was 40%, Aspergillus aculeatus was 60% and Aspergillus flavus was 20% while Fusarium moniliforme was 80% and Fusarium redolens was 40%. The result demonstrated that three species of the fungal isolates Aspergillus aculeatus, Aspergillus carneus and Fusarium moniliforme were found to produce amylases. Aspergillus aculeatus isolated from locations C3, D1 and D2 produced 0.018mg/ml, 0.018mg/ml and 0.016mg/ml amylases respectively. Similarly, Aspergillus carneus isolated from locations A1 and B2 produced 0.021mg/ml and 0.012mg/ml amylases. Fusarium moniliforme isolated from locations A3, C1 and C4 produced 0.010mg/ml, 0.016mg/ml and 0.015mg/ml amylases. Result of effect of (temperature, pH and fermentation time) for production of amylases. Whereas highest amount for amylases produced by Aspergillus aculeatus and F monliforme were produced at 28 OC. pH 5.0 was found to the best optima pH for production of amylases from the fungi studied A. carneus (2.99 mg/ml amylases). The fermentation time showed highest production of amylase by A. carneus and A. aculeatus after 72 hours while F. moniliforme produced at 96hours. The fungi species isolated from soil in keffi can be used for production of amylases.

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Burstyn, Igor, Kay Teschke, Karen Bartlett, and Susan M. Kennedy. "Determinants of Wheat Antigen and Fungal α-Amylase Exposure in Bakeries." American Industrial Hygiene Association Journal 59, no. 5 (May 1998): 313–20. http://dx.doi.org/10.1080/15428119891010569.

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Kanerva, Lasse, Markku Vanhanen, and Outi Tupasela. "Occupational allergic contact urticaria from fungal but not bacterial α-amylase." Contact Dermatitis 36, no. 6 (June 1997): 306. http://dx.doi.org/10.1111/j.1600-0536.1997.tb00007.x.

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Patel, M. J., J. H. Y. Ng, W. E. Hawkins, K. F. Pitts, and S. Chakrabarti-Bell. "Effects of fungal α-amylase on chemically leavened wheat flour doughs." Journal of Cereal Science 56, no. 3 (November 2012): 644–51. http://dx.doi.org/10.1016/j.jcs.2012.08.002.

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Bluhm, B. H., and C. P. Woloshuk. "Amylopectin Induces Fumonisin B1 Production by Fusarium verticillioides During Colonization of Maize Kernels." Molecular Plant-Microbe Interactions® 18, no. 12 (December 2005): 1333–39. http://dx.doi.org/10.1094/mpmi-18-1333.

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Fusarium verticillioides, a fungal pathogen of maize, produces fumonisin mycotoxins that adversely affect human and animal health. Basic questions remain unanswered regarding the interactions between the host plant and the fungus that lead to the accumulation of fumonisins in maize kernels. In this study, we evaluated the role of kernel endosperm composition in regulating fumonisin B1 (FB1) biosynthesis. We found that kernels lacking starch due to physiological immaturity did not accumulate FB1. Quantitative polymerase chain reaction analysis indicated that kernel development also affected the expression of fungal genes involved in FB1 biosynthesis, starch metabolism, and nitrogen regulation. A mutant strain of F. verticillioides with a disrupted α-amylase gene was impaired in its ability to produce FB1 on starchy kernels, and both the wild-type and mutant strains produced significantly less FB1 on a high-amylose kernel mutant of maize. When grown on a defined medium with amylose as the sole carbon source, the wild-type strain produced only trace amounts of FB1, but it produced large amounts of FB1 when grown on amylopectin or dextrin, a product of amylopectin hydrolysis. We conclude that amylopectin induces FB1 production in F. verticillioides. This study provides new insight regarding the interaction between the fungus and maize kernel during pathogenesis and highlights important areas that need further study.

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Kabir, Md Tanvir, Md Shahinur Kabir, Md Kamruzzaman Pramanik, Md Zahidul Islam, and Effat Jahan Tamanna. "Production of chitosan from Oyster mushroom for α-amylase immobilization." Bangladesh Journal of Botany 49, no. 3 (September 20, 2020): 593–99. http://dx.doi.org/10.3329/bjb.v49i3.49989.

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Experiments were carried out to produce chitosan from a locally available mushroom and to use the produced chitosan as a matrix to immobilize α-amylase. On the basis of morphological characteristics and the sequence of the internal transcribed spacer region of the nuclear rDNA, the fungal sample was identified as Pleurotus ostreatus. The average crude chitin content in the dried fruit body of P. ostreatus was 24.11%. The average yield of chitosan from P. ostreatus was 163.3 mg/g dry weight and the degree of deacetylation of the produced chitosan was 73.42%. This chitosan was used as a matrix to immobilize α-amylase. The diameter of the α-amylase immobilized beads ranged from 1839 - 2273 μm. The amount of reducing sugar produced from starch by using free α-amylase and chitosan-immobilized α-amylase was 1.710 and 1.508 mg/ml, respectively. Immobilized enzyme produced only 11.81% less reducing sugar than that of the soluble enzyme in the first cycle. However, immobilized α-amylase was easily recovered from the product and reused for two more cycles which was not possible with the same soluble free enzyme. Considering the total production of reducing sugar in three cycles, chitosan-immobilized α-amylase was found to be more productive and cost-effective than conventional soluble enzymatic reaction.

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Rashid, Naeem, Anjum Shehzad, Nasir Ahmad, Zaheer Hussain, and Muhammad S. Haider. "Valorization of waste foods using pullulan hydrolase from Thermococcus kodakarensis." Amylase 2, no. 1 (December 31, 2018): 39–43. http://dx.doi.org/10.1515/amylase-2018-0005.

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Abstract The starchy foods including staled or leftover bread, insect infested or damaged cereal grains and bakery wastes are usually discarded, which is a threat to public health due to extensive fungal growth. In the present study we have utilized them as raw materials for synthesis of maltose and glucose syrups using pullulan hydrolase from Thermococcus kodakarensis (TK-PUL). The novelty of the process was that whole process was completed: (i) in the absence of any liquefying amylase; (ii) without pre-gelatinization of starch; and (iii) using undisrupted E. coli cells, expressing TK-PUL gene, as a source of extremely thermostable TK-PUL protein. Since glucose and maltose can serve as precursors for a variety of biotechnological products, it is therefore anticipated that hydrolysis of starchy food wastes by TK-PUL would be highly beneficial. It will serve as cost effective measure not only to extract valuables from rubbish but also lower the level of environmental pollutants.

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Codină, Dabija, and Oroian. "Prediction of Pasting Properties of Dough from Mixolab Measurements Using Artificial Neuronal Networks." Foods 8, no. 10 (October 1, 2019): 447. http://dx.doi.org/10.3390/foods8100447.

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An artificial neuronal network (ANN) system was conducted to predict the Mixolab parameters which described the wheat flour starch-amylase part (torques C3, C4, C5, and the difference between C3-C4and C5-C4, respectively) from physicochemical properties (wet gluten, gluten deformation index, Falling number, moisture content, water absorption) of 10 different refined wheat flourssupplemented bydifferent levels of fungal α-amylase addition. All Mixolab parameters analyzed and the Falling number values were reduced with the increased level of α-amylase addition. The ANN results accurately predicted the Mixolab parameters based on wheat flours physicochemical properties and α-amylase addition. ANN analyses showed that moisture content was the most sensitive parameter in influencing Mixolab maximum torque C3 and the difference between torques C3 and C4, while wet gluten was the most sensitive parameter in influencing minimum torque C4 and the difference between torques C5 and C4, and α-amylase level was the most sensitive parameter in predicting maximum torque C5. It is obvious that the Falling number of all the Mixolab characteristics best predicted the difference between torques C3 and C4.

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Gronchi, Nicoletta, Lorenzo Favaro, Lorenzo Cagnin, Silvia Brojanigo, Valentino Pizzocchero, Marina Basaglia, and Sergio Casella. "Novel Yeast Strains for the Efficient Saccharification and Fermentation of Starchy By-Products to Bioethanol." Energies 12, no. 4 (February 22, 2019): 714. http://dx.doi.org/10.3390/en12040714.

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The use of solid starchy waste streams to produce value-added products, such as fuel ethanol, is a priority for the global bio-based economy. Despite technological advances, bioethanol production from starch is still not economically competitive. Large cost-savings can be achieved through process integration (consolidated bioprocessing, CBP) and new amylolytic microbes that are able to directly convert starchy biomass into fuel in a single bioreactor. Firstly, CBP technology requires efficient fermenting yeast strains to be engineered for amylase(s) production. This study addressed the selection of superior yeast strains with high fermentative performances to be used as recipient for future CBP engineering of fungal amylases. Twenty-one newly isolated wild-type Saccharomyces cerevisiae strains were screened at 30 °C in a simultaneous saccharification and fermentation (SSF) set up using starchy substrates at high loading (20% w/v) and the commercial amylases cocktail STARGEN™ 002. The industrial yeast Ethanol Red™ was used as benchmark. A cluster of strains produced ethanol levels (up to 118 g/L) significantly higher than those of Ethanol Red™ (about 109 g/L). In particular, S. cerevisiae L20, selected for a scale-up process into a 1-L bioreactor, confirmed the outstanding performance over the industrial benchmark, producing nearly 101 g/L ethanol instead of 94 g/L. As a result, this strain can be a promising CBP host for heterologous expression of fungal amylases towards the design of novel and efficient starch-to-ethanol routes.

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Vaish, S., N. Garg, and I. Z. Ahmad. "Bioprospecting of microbial isolates from biodynamic preparations for PGPR and biocontrol properties." Journal of Environmental Biology 42, no. 3 (May 4, 2021): 644–51. http://dx.doi.org/10.22438/jeb/42/3/mrn-1529.

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Aim: To study the role of microorganisms behind their bioenhancing, biocontrol properties, their enzymatic potential, and characterization of high performing microbial isolates on molecular basis. Methodology: Dominant culturable microbes including bacteria and fungi were isolated from biodynamic preparations and screened on the basis of plant-growth promoting (PGP) activities viz., ammonia production, phosphate solubilization, siderophore production, hydrogen cyanide production, seed germination efficacy and biocontrol properties. The dominant and effective microorganisms were screened for enzymes activities viz., pectinase, cellulase and amylase. The selected bacterial and fungal isolates, exhibiting higher enzyme activities, were subjected to molecular characterization. Results: Out of 68 bacterial and 25 fungal isolates from 8 biodynamic preparations (BD 500 - BD 507), 15 bacterial isolates exhibited high plant growth promoting activities while 10 bacterial isolates exhibited biocontrol activity against pathogens. Bacillus licheniformis isolated from BD 504, expressed high pectinase (2.595 U ml-1 min-1), cellulase (0.308 U ml-1 min-1) and amylase (0.418 U ml-1 min-1) activities. Fungal isolates with high enzymatic activities, were isolated from BD 500, 503 and 506, respectively. Interpretation: Microorganism isolates from biodynamic preparations possessed strong plant growth promoting, biocontrol and enzymatic properties, which might be responsible for the efficacy of organic preparations under field conditions.

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Avwioroko, Oghenetega, Akpovwehwee Anigboro, and Nyerhovwo Tonukari. "Biotechnological Application of Cassava-Degrading Fungal (CDF) Amylase in Broiler Feed Formulation." British Biotechnology Journal 10, no. 1 (January 10, 2016): 1–12. http://dx.doi.org/10.9734/bbj/2016/20614.

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Shah, N. K., V. Ramamurthy, and R. M. Kothari. "Comparative profiles of fungal alpha amylase production by submerged and surface fermentation." Biotechnology Letters 13, no. 5 (May 1991): 361–64. http://dx.doi.org/10.1007/bf01027683.

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Sander, I., E. Zahradnik, J. Bogdanovic, M. Raulf-Heimsoth, I. M. Wouters, A. Renström, J. Harris-Roberts, et al. "Optimized methods for fungal ?-amylase airborne exposure assessment in bakeries and mills." Clinical & Experimental Allergy 37, no. 8 (August 2007): 1229–38. http://dx.doi.org/10.1111/j.1365-2222.2007.02756.x.

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Lillienberg, L. "Comparison of four methods to assess fungal Î±-amylase in flour dust." Annals of Occupational Hygiene 44, no. 6 (September 2000): 427–33. http://dx.doi.org/10.1016/s0003-4878(99)00118-0.

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Tintu, Ignatius, Kalarickal Vijayan Dileep, Chandran Remya, Anu Augustine, and Chittalakkottu Sadasivan. "6-Gingerol inhibits fungal alpha amylase: Enzyme kinetic and molecular modeling studies." Starch - Stärke 64, no. 8 (April 23, 2012): 607–12. http://dx.doi.org/10.1002/star.201200004.

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Adeniran, H. A., S. H. Abiose, and A. O. Ogunsua. "Production of Fungal β-amylase and Amyloglucosidase on Some Nigerian Agricultural Residues." Food and Bioprocess Technology 3, no. 5 (September 16, 2008): 693–98. http://dx.doi.org/10.1007/s11947-008-0141-3.

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Demirel, R., N. Yılmaz Sarıözlü, and S. İlhan. "Production of fungal amylase enzyme from Aspergillus species in solid-state culture." Journal of Biotechnology 136 (October 2008): S31. http://dx.doi.org/10.1016/j.jbiotec.2008.07.059.

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Møller, Kasper, Mostafa Z. Sharif, and Lisbeth Olsson. "Production of fungal α-amylase by Saccharomyces kluyveri in glucose-limited cultivations." Journal of Biotechnology 111, no. 3 (August 2004): 311–18. http://dx.doi.org/10.1016/j.jbiotec.2004.04.013.

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Sheehan, Helen, and Barry V. McCleary. "A new procedure for the measurement of fungal and bacterial α-amylase." Biotechnology Techniques 2, no. 4 (December 1988): 289–92. http://dx.doi.org/10.1007/bf01875544.

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Lacerda, L. G., M. A. da Silva Carvalho Filho, I. M. Demiate, G. Bannach, M. Ionashiro, and E. Schnitzler. "Thermal behaviour of corn starch granules under action of fungal α-amylase." Journal of Thermal Analysis and Calorimetry 93, no. 2 (July 22, 2008): 445–49. http://dx.doi.org/10.1007/s10973-006-8273-z.

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Kirisanth, Annalingam, M. N. M. Nafas, Ranga K. Dissanayake, and Jayantha Wijayabandara. "Antimicrobial and Alpha-Amylase Inhibitory Activities of Organic Extracts of Selected Sri Lankan Bryophytes." Evidence-Based Complementary and Alternative Medicine 2020 (July 22, 2020): 1–6. http://dx.doi.org/10.1155/2020/3479851.

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Medicinal plants have been the main focus of natural product research. However, recent research has revealed that lower plants including bryophytes are also a major resource of biologically active compounds with novel structures. Sri Lanka is considered as a biodiversity hotspot with a higher degree of endemism flora including bryophytes. In this study, different species of bryophytes were investigated for their antimicrobial and alpha-amylase inhibitory activities. The air-dried plant materials of 6 different bryophyte species, Marchantia sp., Fissidens sp., Plagiochila sp., Sematophyllum demissum, Hypnum cupressiforme, and Calymperes motley, were subjected to sequential cold extraction with 3 different organic solvents. All three types of organic crude extracts were subjected to screening of antimicrobial bioassays using the disc-diffusion method against 3 bacterial strains and 1 fungal strain. According to the results obtained, 6 extracts out of 18 showed antibacterial activity for tested Gram-positive bacteria and 1 active against Gram-negative bacteria. Two extracts showed activity against the pathogenic fungus strain. Extracts from some plants were active against tested bacterial as well as fungal species. TLC-based bioautographic study was carried out to identify the corresponding active bands which is useful for active compound isolation. Furthermore, the ethyl acetate extracts were subjected to evaluate alpha-amylase inhibitory activity where three extracts out of six extracts showed moderate inhibitory activity for alpha-amylase with IC50 ranging 8–30%.

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Journal articles on the topic 'Fungal amylase'

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