Purification and characterization of an extracellular amylase from <i>Lactobacillus plantarum</i> strain A6

Giraud, Éric; Gosselin, Laurent; Marin, Bernard; Parada, José; Raimbault, Maurice

doi:10.1111/j.1365-2672.1993.tb02777.x

Cited by 71 publications

(40 citation statements)

References 16 publications

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“…The fold purification and yields were comparable to those reported previously; for example, extracellular α-amylase of Lactobacillus plantarum A6 (50-70%) was purified to 35.6% yield with 19.5-fold purification by 40-80% ammonium sulfate precipitation and diethyl aminoethyl anion exchange chromatography 14 …”

Section: Resultssupporting

confidence: 63%

Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain

Baltaş

Dinçer

Ekinci

et al. 2016

Braz. arch. biol. technol.

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Section: Resultssupporting

confidence: 63%

Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain

Baltaş

Dinçer

Ekinci

et al. 2016

Braz. arch. biol. technol.

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“…The desired band size for amylase of 50 KDa was obtained ( Figure 6). Amylase enzymes with same molecular weight was reported in the previous literature [15,16]. These results revealed that Bacillus Subtilis strain identified for amylase production from salt mines of Karak will be a good option for those industrial applications have high pH and temperature as common laboratory conditions.…”

Section: Partial Purification Of Amylasessupporting

confidence: 70%

Molecular characterization and growth optimization of halo-tolerant amylase producing bacteria isolated from salt mines of Karak, Pakistan

Shah

Qasim

Rahman

et al. 2017

PAB

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Microorganisms are commonly used for the production of different types of enzymes, among which amylases are extensively used for different industrial purposes like food industry, paper industry, textile industry and detergents etc. In this study, extremophilic bacteria were isolated from salt mines of Karak, Pakistan which have the ability to grow and express amylases at diverse environmental conditions. In Total, 43 out of the 53 bacteria were found positive for amylase production. Furthermore, microscopic, biochemical and phylogenetic analysis inferred from 16S rRNA gene sequencing identified that amylase producing strain SBA-5 belong to Bacillus subtilis. The strain SBA-5 identified as Bacillus subtilis exhibited high amylase production at pH 9 and temperature 37°C. The present study revealed that the salt mines of Karak have high population of halotolerant microorganism feasible for use under diverse environmental conditions, which can be of great importance for various bio-industrial applications.

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“…Reducing sugars were quantified by the DNS method by using glucose as a standard (31). One unit of amylase activity was defined as the amount of enzyme that liberated 1 mol of glucose per s. In addition, ␣-amylase activity on soluble potato starch was determined by measuring its iodine-complexing ability according to the protocol described by Giraud et al (12).…”

Section: Methodsmentioning

confidence: 99%

Starch-Binding Domain Affects Catalysis in Two Lactobacillus α-Amylases

Rodríguez‐Sanoja

Ruiz²,

Guyot³

et al. 2005

Appl Environ Microbiol

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A new starch-binding domain (SBD) was recently described in ␣-amylases from three lactobacilli (Lactobacillus amylovorus, Lactobacillus plantarum, and Lactobacillus manihotivorans). Usually, the SBD is formed by 100 amino acids, but the SBD sequences of the mentioned lactobacillus ␣-amylases consist of almost 500 amino acids that are organized in tandem repeats. The three lactobacillus amylase genes share more than 98% sequence identity. In spite of this identity, the SBD structures seem to be quite different. To investigate whether the observed differences in the SBDs have an effect on the hydrolytic capability of the enzymes, a kinetic study of L. amylovorus and L. plantarum amylases was developed, with both enzymes acting on several starch sources in granular and gelatinized forms. Results showed that the amylolytic capacities of these enzymes are quite different; the L. amylovorus ␣-amylase is, on average, 10 times more efficient than the L. plantarum enzyme in hydrolyzing all the tested polymeric starches, with only a minor difference in the adsorption capacities.␣-Amylases (1,4-␣-D-glucan-4 glucanohydrolase; EC 3.2.1.1) are a widespread group of enzymes that catalyze the hydrolysis of the ␣-1,4 glycosidic linkages of raw and soluble starch, thereby generating smaller dextrins and oligosaccharides. They are classified into family 13 in the sequence-based classification of glycoside hydrolases (GH-13) (16, 17). They are multidomain proteins that contain, in addition to the catalytic (␤/␣) 8 domain (domain A), domains B and C. Domain B is inserted between the third ␤-strand and the third ␣-helix of the barrel and varies greatly in length and structure (21). Domain C follows the catalytic barrel; this domain is made of ␤-strands and is thought to stabilize the catalytic domain by shielding hydrophobic residues of domain A from the solvent (29). Some of these enzymes contain one noncatalytic domain whose function is generally described as that of a starch-binding domain (SBD).The SBD is a functional domain that can bind granular starch, increasing the local concentration of substrate at the active site of the enzyme, and that may also disrupt the structure of the starch surface, thereby enhancing the amylolytic rate (39, 40). In the primary structure classification of glycoside hydrolases (16, 17; http://afmb.cnrs-mrs.fr/ϳcazy/CAZY/index .html), the carbohydrate-binding modules (CBM) are organized into 39 families, which include several specificities such as cellulose, xylan, chitin, and starch binding. The most generalized and studied family of starch-binding modules is CBM-20. These modules are present in approximately 10% of amylolytic enzymes from GH-13 (almost all cyclomaltodextrin glucanotransferase, in a few ␣-amylases, and in maltotetraohydrolases, maltopentaohydrolases, maltogenic ␣-amylases, and acarviose transferases), GH-14 (some ␤-amylases), and GH-15 (most fungal glucoamylases). This domain is positioned at the C-terminal end of proteins except for the glucoamylase from Rhizopus oryzae and the The...

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Purification and characterization of an extracellular amylase from Lactobacillus plantarum strain A6

Cited by 71 publications

References 16 publications

Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain

Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain

Molecular characterization and growth optimization of halo-tolerant amylase producing bacteria isolated from salt mines of Karak, Pakistan

Starch-Binding Domain Affects Catalysis in Two Lactobacillus α-Amylases

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