Characterization of a Novel Maltose-Forming α-Amylase from <i>Lactobacillus plantarum</i> subsp. <i>plantarum</i> ST-III

Jeon, Hye-Yeon; Kim, Nari; Lee, Hye Won; Choi, Ho‐Young; Choung, Woo-Jae; Koo, Ye-Seul; Ko, Dam-Seul; Shim, Jae‐Hoon

doi:10.1021/acs.jafc.5b05892

Cited by 25 publications

(17 citation statements)

References 47 publications

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“…Amy2 from L. plantarum subsp. plantarum ST-III has been previously characterized and its maltose-forming α-amylase activity described [7]. Amy2 from this strain has an amino acid sequence identical to Lp_0179 (Amy2) from L. plantarum WCFS1 (data not shown).…”

Section: Resultsmentioning

confidence: 95%

“…This result confirmed that both enzymes hydrolysed α-1,4-glucosidic bonds. However, the activity of Lp_0179 (LpMA) on p NP-α- d -maltopentaoside was previously analysed reporting that Lp_0179 hydrolyzed the α-1,4-glucosidic bonds of p NP-α- d -maltopentaoside, resulting in production of maltose and p NP-α- d -maltotriose [7]. This result could be in agreement with the results reported in our study, as Lp_0179 was unable to liberate p NP (detected colorimetrically) but able to hydrolyze one internal α-1,4-glucosidic bond to liberate p NP-α- d -maltotriose and maltose (detected by HPAEC and thin layer chromatography) [7].…”

Section: Resultsmentioning

confidence: 99%

“…In this regard, the objective of this study was to determine the functional features of the putative Lp_2757 maltogenic α-amylase from L. plantarum WCFS1, through biochemical characterization of the recombinantly expressed protein. Moreover, as a maltose-forming α-amylase has been previously described from L. plantarum [7], a detailed comparison among the two L. plantarum amylolytic proteins has been also carried out.…”

Section: Introductionmentioning

confidence: 99%

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Unravelling the diversity of glycoside hydrolase family 13 α-amylases from Lactobacillus plantarum WCFS1

et al. 2019

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Backgroundα-Amylases specifically catalyse the hydrolysis of the internal α-1, 4-glucosidic linkages of starch. Glycoside hydrolase (GH) family 13 is the main α-amylase family in the carbohydrate-active database. Lactobacillus plantarum WCFS1 possesses eleven proteins included in GH13 family. Among these, proteins annotated as maltose-forming α-amylase (Lp_0179) and maltogenic α-amylase (Lp_2757) were included.ResultsIn this study, Lp_0179 and Lp_2757 L. plantarum α-amylases were structurally and biochemically characterized. Lp_2757 displayed structural features typical of GH13_20 subfamily which were absent in Lp_0179. Genes encoding Lp_0179 (Amy2) and Lp_2757 were cloned and overexpressed in Escherichia coli BL21(DE3). Purified proteins showed high hydrolytic activity on pNP-α-D-maltopyranoside, being the catalytic efficiency of Lp_0179 remarkably higher. In relation to the hydrolysis of starch-related carbohydrates, Lp_0179 only hydrolysed maltopentaose and dextrin, demonstrating that is an exotype glucan hydrolase. However, Lp_2757 was also able to hydrolyze cyclodextrins and other non-cyclic oligo- and polysaccharides, revealing a great preference towards α-1,4-linkages typical of maltogenic amylases.ConclusionsThe substrate range as well as the biochemical properties exhibited by Lp_2757 maltogenic α-amylase suggest that this enzyme could be a very promising enzyme for the hydrolysis of α-1,4 glycosidic linkages present in a broad number of starch-carbohydrates, as well as for the investigation of an hypothetical transglucosylation activity under appropriate reaction conditions.

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Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Unravelling the diversity of glycoside hydrolase family 13 α-amylases from Lactobacillus plantarum WCFS1

et al. 2019

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“…Previous studies showed that L. plantarum has amylolytic activity up to 20 U/ml and cellulolytic activity up to 12 U/ml after 18 h of fermentation at a steady temperature of 37°C during cassava fermentation [27]. Enzyme amylase activity from L. plantarum also has been observed by several researchers [29][30][31]. Cellulolytic property of microorganism is essential for breaking down the cell wall of cassava roots, resulting in improving physical properties of a mocaf product.…”

Section: Fermentationmentioning

confidence: 91%

Microbial Fermentation as Means of Improving Cassava Production in Indonesia

Frediansyah¹

2018

Cassava

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Cassava is one of the pivotal carbohydrate sources for millions of people in Indonesia. Its production up to 20 million ton a year made this country to become the third most prominent producer of cassava. However, cassava is often considered as food sources for marginal people. The majority of individuals still depend on rice and wheat flour for carbohydrate intake. Unfortunately, the elevating consumption of those sources is an imbalance with its products nationally. Both use of rice product and wheat flour is more than 8.5 kg/capita/year. The critical fact is that Indonesia is one of the biggest countries in rice production globally. However, it is also one of the largest, rice importers. Another hand, the existence of wheat flour is the result of imports from other countries and always increasing every year. The Indonesian government has contributed actively to resuscitate local foods including the cassava. There are numerous strategies that have been applied to substitute the wheat flour, however, the characteristic was always far different from its flour. Mocaf is the recent trend for Indonesian food industry. It is free of gluten and can easily substitute with wheat flour to produce several types of wheat-dependent-products.

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“…Although D. fristingensis is a psychrotolerant yeast having an optimal growth temperature at 15°C, its secreted α-glucosidase exhibit the best activity at 37-40°C having its K m value on soluble starch of 1.3 g/L. This K m value is in the range typical for microbial α-amylases and glucoamylases described to be best active at 40-50°C, but is lower than that for the enzymes with optimal activity above 60°C [13,[48][49][50]. In relation to thermal inactivation of the α-glucosidase from D. fristingensis, its decimal reduction time at 30°C, 40°C and 50°C was 12.5, 10.5 and 7 h, respectively.…”

Section: Thermal Inactivation Of D Fristingensis α-Glucosidasementioning

confidence: 97%

Purification and characterization of a novel α-glucosidase from an Antarctic yeast Dioszegia fristingensis isolate

Carrasco

Alcaı́no

Cifuentes

et al. 2017

Amylase

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Starch hydrolyzing enzymes, amylases, are important commercial enzymes used in several productive areas. A current tendency is to find amylases with high catalytic activity at 20-40°C, to generate products that work well at low temperatures, such as detergents, and for energy saving resources in industrial processes. In this work, an α-glucosidase secreted by the cold-adapted yeast Dioszegia fristingensis was purified and biochemically characterized. The effect of physicochemical parameters on the enzyme activity was evaluated. According to our results, the amylolytic enzyme secreted by D. fristingensis is a monomeric α-glucosidase of about 30 kDa that displayed the highest activity at 37-40°C and at pH 5.5-6.5,in the presence of 10 mM CaCl

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Characterization of a Novel Maltose-Forming α-Amylase from Lactobacillus plantarum subsp. plantarum ST-III

Cited by 25 publications

References 47 publications

Unravelling the diversity of glycoside hydrolase family 13 α-amylases from Lactobacillus plantarum WCFS1

Unravelling the diversity of glycoside hydrolase family 13 α-amylases from Lactobacillus plantarum WCFS1

Microbial Fermentation as Means of Improving Cassava Production in Indonesia

Purification and characterization of a novel α-glucosidase from an Antarctic yeast Dioszegia fristingensis isolate

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