Extracellular Production and Characterization of Streptomyces X-prolyl Dipeptidyl Aminopeptidase

Hatanaka, Tadashi; Yamasato, Akihiro; Arima, Jiro; Usuki, Hirokazu; Yamamoto, Yukihiro; Kumagai, Yuya

doi:10.1007/s12010-010-9149-z

Cited by 10 publications

(9 citation statements)

References 23 publications

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“…fuscus NBRC 14270 Another pharmaceutically valuable enzyme, X-prolyl-dipeptidyl aminopeptidase (XDAP) is known to be produced by thermophilic Streptomyces sp. (Hatanaka et al, 2011b ), which acts on proline rich proteins and produces short peptides. These peptides act as inhibitors of dipeptidyl peptidase-4 (DPP-IV) and can regulate the blood sugar levels as DPP-IV degrades glucagon like protein-1 (GLP-1) which regulates insulin production and lowers the blood sugar level.…”

Section: Applications Of Thermophilic and Alkaliphilic Actinobacteriamentioning

confidence: 99%

Thermophilic and alkaliphilic Actinobacteria: biology and potential applications

2015

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Microbes belonging to the phylum Actinobacteria are prolific sources of antibiotics, clinically useful bioactive compounds and industrially important enzymes. The focus of the current review is on the diversity and potential applications of thermophilic and alkaliphilic actinobacteria, which are highly diverse in their taxonomy and morphology with a variety of adaptations for surviving and thriving in hostile environments. The specific metabolic pathways in these actinobacteria are activated for elaborating pharmaceutically, agriculturally, and biotechnologically relevant biomolecules/bioactive compounds, which find multifarious applications.

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Section: Applications Of Thermophilic and Alkaliphilic Actinobacteriamentioning

confidence: 99%

Thermophilic and alkaliphilic Actinobacteria: biology and potential applications

2015

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“…chrysanthemi 3,937 (118.7 U/mg) (Kotzia & Labrou, ), Aquabacterium sp . A7‐Y (458.9 U/mg) (Sun et al, ), Streptomyces thermoluteus (68.3 U/mg) and S. griseus (48.9 U/mg) (Hatanaka et al, ), but it is lower than the specific activity of the archaea L‐asparaginases (Chohan & Rashid, ; Zuo, Zhang, Jiang, & Mu, ). The enzyme activity of srnASNase toward L‐asparagine was considered as 100%.…”

Section: Resultsmentioning

confidence: 99%

“…S. griseus (48.9 U/mg) (Hatanaka et al, 2011), but it is lower than the specific activity of the archaea L-asparaginases (Chohan & Rashid, 2013;Zuo, Zhang, Jiang, & Mu, 2015b). The enzyme activity of sr-nASNase toward L-asparagine was considered as 100%.…”

Section: Enzymatic Properties Of Asparaginasementioning

confidence: 99%

Antitumor activity and ability to prevent acrylamide formation in fried foods of asparaginase from soybean root nodules

2019

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A novel asparaginase (designated srnASNase) has been purified from soybean root nodules and identified by MALDI‐TOF/TOF‐MS. And the enzymatic properties, antitumor activity and the ability to prevent acrylamide formation in fried foods of srnASNase were evaluated. SrnASNase had high specific activity (531.37 U/mg) toward L‐asparagine under optimum conditions (pH 8.0 and 40°C), no activity toward L‐glutamine and D‐glutamine, but trace activity toward D‐asparagine. It was stable in the pH range of 7.0–9.0 and up to 40°C. The Km and Vmax of srnASNase were 0.36 mM and 51.64 mM/min, respectively. Further, in vitro anti‐proliferative activity on human cancer cells assay showed that srnASNase was superior to commercial asparaginase in solution by controlling the tumor cell growth with time. In addition, srnASNase showed more effective acrylamide mitigation than commercial asparaginase in fried foods. These results indicate that srnASNase is a potential candidate for applications in the food processing and pharmaceutical industry. Practical applications L‐asparaginase (L‐asparagine amidohydrolase; EC 3.5.1.1) is an enzyme that catalyzes the hydrolysis of the amide group of the side‐chain of L‐asparagine into aspartic acid and ammonia. It has long been used as a primary component in the treatment of acute lymphoblastic leukemia (All) and other related blood cancers. Apart from its clinical usage, L‐asparaginase has attracted more attention in the food processing industries as a promising acrylamide‐mitigating agent in recent years. This research revealed that soybean root nodules might be good sources of novel asparaginase.

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“…Aminopeptidas e (HP1037) – Enzyme activities toward amino acidic derivatives (Xaa) of p -nitroanilide (Xaa- p NA) derivatives were determined in a 96-well microtiter plate by adding an enzyme solution (0–20 nM) and a substrate solution in DMSO (1–20 mM) in a final volume of 200 µl and continuously monitored the increase in absorption at 405 nm caused by the release of p -nitroaniline [18]. The initial activity rate was determined from the linear part of the optical density profile (ε 405nm of 10600 M −1 cm −1 ).…”

Section: Methodsmentioning

confidence: 99%

Biochemical Characterization of Hypothetical Proteins from Helicobacter pylori

Choi

Juárez²,

Ciordia³

et al. 2013

PLoS ONE

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The functional characterization of Open Reading Frames (ORFs) from sequenced genomes remains a bottleneck in our effort to understand microbial biology. In particular, the functional characterization of proteins with only remote sequence homology to known proteins can be challenging, as there may be few clues to guide initial experiments. Affinity enrichment of proteins from cell lysates, and a global perspective of protein function as provided by COMBREX, affords an approach to this problem. We present here the biochemical analysis of six proteins from Helicobacter pylori ATCC 26695, a focus organism in COMBREX. Initial hypotheses were based upon affinity capture of proteins from total cellular lysate using derivatized nano-particles, and subsequent identification by mass spectrometry. Candidate genes encoding these proteins were cloned and expressed in Escherichia coli, and the recombinant proteins were purified and characterized biochemically and their biochemical parameters compared with the native ones. These proteins include a guanosine triphosphate (GTP) cyclohydrolase (HP0959), an ATPase (HP1079), an adenosine deaminase (HP0267), a phosphodiesterase (HP1042), an aminopeptidase (HP1037), and new substrates were characterized for a peptidoglycan deacetylase (HP0310). Generally, characterized enzymes were active at acidic to neutral pH (4.0–7.5) with temperature optima ranging from 35 to 55°C, although some exhibited outstanding characteristics.

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Extracellular Production and Characterization of Streptomyces X-prolyl Dipeptidyl Aminopeptidase

Cited by 10 publications

References 23 publications

Thermophilic and alkaliphilic Actinobacteria: biology and potential applications

Thermophilic and alkaliphilic Actinobacteria: biology and potential applications

Antitumor activity and ability to prevent acrylamide formation in fried foods of asparaginase from soybean root nodules

Biochemical Characterization of Hypothetical Proteins from Helicobacter pylori

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