Characteristics and production of thermostable α-amylase

Kindle, Karen L.

doi:10.1007/bf02778096

Cited by 43 publications

(18 citation statements)

References 102 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The K~ for the first substrate was 6.2 mg/ml and for the second 7.7 mg/ml, whereas the catalytic constants (K~t) were 1432 s -~ and 1069 s -~, respectively. These Km values are higher than the corresponding Km values for porcine pancreas (1.4 mg/ml) (Levitzki and Steer 1974) and bacilli (0.8-1.6 mg/ml) (Kindle 1983) …”

Section: Resultsmentioning

confidence: 57%

Extracellular α-amylase from Streptomyces rimosus

Vukelić

Ritonja

Renko

et al. 1992

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

A purification procedure for an extracellular alpha-amylase from Streptomyces rimosus, oxytetracycline-producing strain, is described. The enzyme obtained was shown to be an acidic (pI 4.75) monomer with a relative molecular mass (M(r)) of 43,000, containing three cysteines involved in the catalytic activity of the enzyme. Its amino-terminal part has 57-67% homology with amylases from other Streptomyces species. S. rimosus alpha-amylase is sensitive to higher temperatures, and partially stabilized by Ca2+ ions. It hydrolyses starch (optimum at pH 5.0-6.0) in an endohydrolase manner giving rise to maltotriose, maltotetraose and higher oligosaccharides. Starch granules, except those from rice, were not significantly affected by the isolated alpha-amylase.

show abstract

Section: Resultsmentioning

confidence: 57%

Extracellular α-amylase from Streptomyces rimosus

Vukelić

Ritonja

Renko

et al. 1992

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…α-amylase have been reported by Acinetobacter spp., Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus megaterium, Bacillus subtilis and some thermophilic actinomycetes organisms as well, for example, Thermomonospora curvata and Thermomonospora vulgaris [2,3], while β-amylase have been reported to be produced by Bacillus cereus, Bacillus circulans, B. megaterium and Paenibacillus polymyxa [4,5]. Lastly,for γ-amylase, in addition to the Bacillus species, halophylic Halolactibacillus sp.…”

Section: Amylasementioning

confidence: 99%

Enzyme Dynamic in Plant Nutrition Uptake and Plant Nutrition

Turan¹,

Nikerel²,

Kaya³

et al. 2017

Enzyme Inhibitors and Activators

View full text Add to dashboard Cite

Soil contains enzymes, constantly interacting with soil constituents, e.g. minerals, rhizosphere and numerous nutrients. Enzymes, in turn, catalyse important biochemical reactions for rhizobacteria and plants, stabilize the soil by degrading wastes and mediate nutrient recycling.The available enzymes inside soil could originate from plants, animals or microbes. The enzymes that are produced from these organism could exhibit intracellular activities, at the cell membrane, interacting therefore with soil and its constituents, or extracellularly (so freely available). Therefore, vis-à-vis to plant nutrition, the (extra or sub) cellular localization has a key role. Typical major enzymes available in soil can be listed as dehydrogenases, hydrogenases, oxidases, catalases, peroxidases, phenol o-hydroxylase, dextransucrase, aminotransferase, rhodanese, carboxylesterase, lipase, phosphatase, nuclease, phytase, arylsulphatase, amylase, cellulase, inulase, xylanase, dextranase, levanase, poly-galacturonase, glucosidase, galactosidase, invertase, peptidase, asparaginase, glutaminase, amidase, urease, aspartate decarboxylase, glutamate decarboxylase and aromatic amino acid decarboxylase. An interesting strategy for improving the nutritional quality of the soil would be to inoculate microorganism to soil while giving attention to mineral or other compounds that affect enzyme activity in soil. Since, some elements or compounds could show both activation and inhibitory effect, such as Fe, Na, etc. metals, the regulation of their bioavailability is crucial.

show abstract

“…Thus as shown in Table 3, with increase in the temperature the kinetic energy increases which corresponds to the increase in the collisions between the substrate and the enzyme resulting in enzyme-substrate complex (Lehninger et al, 2005 andMohammadi et al, 2010). Therefore with increase in temperature initially the enzyme activity increases and it may remain stable at a broad range of its optimal temperature (Prakash et al, 2010 andKindle et al, 1983). If the temperature is increased beyond this then it ruptures the secondary, tertiary and quaternary bonds leading to denaturation of the enzyme (Ciobanu et al, 1976 andSchokker et al, 1999).…”

Section: Effect Of Temperature On Amylase Activitymentioning

confidence: 99%

Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application

Sachdev

Ojha

Mishra

2016

Int J Appl Sci Biotechnol

View full text Add to dashboard Cite

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.

show abstract

Characteristics and production of thermostable α-amylase

Cited by 43 publications

References 102 publications

Extracellular α-amylase from Streptomyces rimosus

Extracellular α-amylase from Streptomyces rimosus

Enzyme Dynamic in Plant Nutrition Uptake and Plant Nutrition

Bacillus Spp. Amylase: Production, Isolation, Characterisation and Its Application

Contact Info

Product

Resources

About