Molecular Cloning and Characterization of an α-Amylase from<i>Pichia burtonii</i>15-1

Kato, Saemi; Shimizu‐Ibuka, Akiko; Mura, Kiyoshi; Takeuchi, Akiko; Tokue, Chiyoko; Arai, Soichi

doi:10.1271/bbb.70407

Cited by 12 publications

(7 citation statements)

References 30 publications

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“…This is also reported by Beech and Davenport (1970) Takeuchi et al (2006) suggested that H. burtonii has positive amylolytic activities Katos et al (2007) sugessted that H. burtonii produce alpha amylas enzyme. Therefore H. burtonii would be good candidate yeast for coffee waste fermentation via acid hydrolysis into simple sugar or other fermentation activities.…”

Section: H Valbyensis Kloeckersupporting

confidence: 74%

Isolation, identification and characterization of yeast species from coffee waste collected from Sidama and Gedio zone

Gizaw¹,

Tsegaye²,

Tefera³

2016

J. Yeast Fungal Res.

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Section: H Valbyensis Kloeckersupporting

confidence: 74%

Isolation, identification and characterization of yeast species from coffee waste collected from Sidama and Gedio zone

Gizaw¹,

Tsegaye²,

Tefera³

2016

J. Yeast Fungal Res.

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“…This enzyme uses a pair of catalytic active site residues (Asp206 as a nucleophile and Glu230 as the acid/base) to cleave amylose chains and requires several subsites to be occupied to catalyze hydrolysis at meaningful rates. 39 To assess time-dependent inhibition, the hydrolysis of 2chloro-4-nitrophenyl maltotrioside (CNP-M3) by Takaamylase was measured after preincubation with 2 mM of inhibitors 1a, 1b, 2a, and 3a. All four inhibitors displayed a time-dependent inhibition of Taka-amylase; however the rates of inhibition varied greatly (Figure 2).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…This suggests that initial binding of 1b is aided by interactions between the −3 subsite and the 4′-alkylamine present, which in turn increases the rate of inhibition. Previous kinetic analysis of Taka-amylase catalytic rates has shown dramatic rate increases for the hydrolysis of a maltotetrasaccharide over a maltotrioside, 39 highlighting the importance of binding in the −3 position with a natural substrate.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…Taka-amylase, one of the earliest amylases to be characterized and used commercially, , is a retaining α-amylase belonging to the GH13 subfamily 1. This enzyme uses a pair of catalytic active site residues (Asp206 as a nucleophile and Glu230 as the acid/base) to cleave amylose chains and requires several subsites to be occupied to catalyze hydrolysis at meaningful rates …”

Section: Results and Discussionmentioning

confidence: 99%

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Activity-Based Protein Profiling of Retaining α-Amylases in Complex Biological Samples

et al. 2021

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Amylases are key enzymes in the processing of starch in many kingdoms of life. They are important catalysts in industrial biotechnology where they are applied in, among others, food processing and the production of detergents. In man amylases are the first enzymes in the digestion of starch to glucose and arguably also the preferred target in therapeutic strategies aimed at the treatment of type 2 diabetes patients through down-tuning glucose assimilation. Efficient and sensitive assays that report selectively on retaining amylase activities irrespective of the nature and complexity of the biomaterial studied are of great value both in finding new and effective human amylase inhibitors and in the discovery of new microbial amylases with potentially advantageous features for biotechnological application. Activity-based protein profiling (ABPP) of retaining glycosidases is inherently suited for the development of such an assay format. We here report on the design and synthesis of 1,6- epi -cyclophellitol-based pseudodisaccharides equipped with a suite of reporter entities and their use in ABPP of retaining amylases from human saliva, murine tissue as well as secretomes from fungi grown on starch. The activity and efficiency of the inhibitors and probes are substantiated by extensive biochemical analysis, and the selectivity for amylases over related retaining endoglycosidases is validated by structural studies.

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“…These effects 333 are driven by three key physiological parameters: the affinity of cells for hydrolyzed 334 oligosaccharide, the rate of polysaccharide hydrolysis, and the amount of exchange on/off the 335 particle surface that define a tradeoff between the rate of polysaccharide degradation and 336 biomass yield. These features contrast with a common assumption of carbon flux models: that 337 model heterotrophic cells consume nutrients at rates comparable to the consumption of simple 338 dissolved substrates by laboratory-adapted model organisms in a well-mixed systems (27)(28)(29). In 339 particular, our computational and experimental results highlight that the frequency at which cells 340 exchange on and off the polysaccharide surface has a large impact on cell carbon uptake.…”

mentioning

confidence: 75%

Cooperation and spatial self-organization determine ecosystem function for polysaccharide-degrading bacteria

Ebrahimi

Schwartzman

Cordero

2019

Preprint

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The recycling of particulate organic matter (POM) by microbes is a key part of the global carbon cycle, one which is mediated by the extracellular hydrolysis of polysaccharides and the production of public goods that can trigger social behaviors in bacteria. Despite the potential importance of these microbial interactions, their role in regulating of ecosystem function remains unclear. In this study, we developed a computational and experimental model system to address this challenge and studied how POM depolymerization rate and carbon use efficiency -two main ecosystem function parameters-depended on social interactions and spatial self-organization on particle surfaces. We found an emergent trade-off between rate and efficiency resulting from the competition between oligosaccharide diffusion and cellular uptake, with low rate and high efficiency being achieved through cell-to-cell cooperation between degraders. Bacteria cooperated by aggregating in cell-clusters of ~10-20µm, where cells were able to share public goods. This phenomenon, which was independent of any explicit group-level regulation, led to the emergence of critical cell concentrations below which degradation did not occur, despite all resources being available in excess. By contrast, when particles were labile and turnover rates were high, aggregation promoted competition and decreased the efficiency of carbon utilization.Our study shows how social interactions and cell aggregation determine the rate and efficiency of particulate carbon turnover in environmentally relevant scenarios.Microorganisms can cooperate by secreting public goods that benefit local neighbors, however, the impact of cooperation on ecosystem functions remains poorly constrained. We here pair computation and experiment to show that bacterial cooperation mediates the degradation of polysaccharide particles recalcitrant to hydrolysis in aquatic environments. On particle surfaces, cooperation emerges through the self-organization of cells into ~10-20µm clusters that promote cooperative uptake of hydrolysis products. The transition between cooperation and competition in aggregates is mitigated by individual cell behaviors such as motility and chemotaxis, that promote reorganization on the particle surface. When cooperation is required, the degradation of recalcitrant biopolymers can only take place when degraders exceed a critical cell concentration, underscoring the importance of microbial interactions for ecosystem function.

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Molecular Cloning and Characterization of an α-Amylase fromPichia burtonii15-1

Cited by 12 publications

References 30 publications

Isolation, identification and characterization of yeast species from coffee waste collected from Sidama and Gedio zone

Isolation, identification and characterization of yeast species from coffee waste collected from Sidama and Gedio zone

Activity-Based Protein Profiling of Retaining α-Amylases in Complex Biological Samples

Cooperation and spatial self-organization determine ecosystem function for polysaccharide-degrading bacteria

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