Actinomycete Enzymes

Peczyńska‐Czoch, Wanda; Mordarski, M

doi:10.1016/b978-0-12-289673-6.50011-7

Cited by 66 publications

(42 citation statements)

References 253 publications

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“…The N-terminal amino acid of the purified alkaline protease was proceeded by a peptide of 15 amino acids in the deduced sequence. We could not find any core of hydrophobic residues and signal cleavage sequence characteristic for a signal peptide 3 ) in this sequence. This suggests that the sequence from the primary translation product could be removed as a consequence of some artifact of the purification as proven for the intracellular serine protease of Bacillus subtilis.…”

Section: Deduced Amino Acid Sequence Of Alkaline Proteasementioning

confidence: 99%

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Cloning and Expression of an Intracellular Alkaline Protease Gene from AlkalopihilicThermoactinomycessp. Η8682

Tsuchiya

Ikeda

Tsuchiya

et al. 1997

Bioscience, Biotechnology, and Biochemistry

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Section: Deduced Amino Acid Sequence Of Alkaline Proteasementioning

confidence: 99%

“…7) Some actinomycetes produce and secrete several kinds of protease in the culture broth, like Pronase from Streptomyces griseus. 3 ) Although we purified only an extracellular alkaline serine protease from the culture broth of Thermoactinomyces sp. HS682,6) we found that this strain produces minor proteases in the cells.…”

mentioning

confidence: 99%

Cloning and Expression of an Intracellular Alkaline Protease Gene from AlkalopihilicThermoactinomycessp. Η8682

Tsuchiya

Ikeda

Tsuchiya

et al. 1997

Bioscience, Biotechnology, and Biochemistry

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“…proteases (Peczynska-Czoch & Mordarski, 1988) as well as protease inhibitors (Aoyagi, 1989). The secretion of extracellular proteolytic enzymes in streptomycetes often temporally coincides with the onset of secondary metabolism or morphological differentiation (Ginther, 1979 ;Gibb & Strohl, 1988;Bascaran e t al., 1990).…”

Section: Streptomycetes Produce a Variety Of Extracellularmentioning

confidence: 99%

Trypsin-like protease of Streptomyces exfoliatus SMF13, a potential agent in mycelial differentiation

Kim

Lee

1996

Microbiology

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Streptomyces exfoliatus SMF13 sequentially produced leupeptin, leupeptininactivating enzyme (LIE) and trypsin-like protease (TLP). TLP was produced upon exhaustion of glucose. Autolysis of mycelium was accompanied by an increase in TLP activity. However, in three bld mutants isolated from 5. exfoliatus SMF13 after UV-mutagenesis, mycelium autolysis did not occur, and neither LIE nor TLP was produced, although leupeptin was produced. Production of both LIE and TLP was restored in a spontaneous Spo+ revertant of a bld mutant. In contrast, two whi mutants sequentially produced leupeptin, LIE and TLP. The molecular mass of TLP produced during morphological differentiation was estimated to be 31.8 kDa by SDS-PAGE. The N-terminal amino acid sequence was RVGGTxAAQGNFPFQQxLSM. TLP was competitively inhibited by leupeptin; the inhibition constant was 0915 pM. TLP effectively hydrolysed the mycelial protein extract of 5. exfoliatus SMF13, but the hydrolytic activity was inhibited by leupeptin. It was concluded that morphological differentiation and production of TLP are coordinately regulated, that TLP may function as an enzyme in the metabolism of mycelial proteins, and that the hydrolytic activity of TLP is regulated by autogenous leupeptin in 5. exfoliafws SMF13.

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“…Among these diverse soil microbial communities, actinobacteria including streptomycetes have occupied a prominent and significant position as potential producers of structurally complex and unique metabolites (Lakshmipathy et al 2010). They are a promising source of a wide range of antibiotics (ATBs), antiparasitic agents, herbicides, anti-cancer drugs, enzyme inhibitors, immunomodifiers, vitamins and various enzymes of industrial importance (Okami & Hotta 1988;Peczynska-Czoch & Mordarski 1988;El-Meleigy et al 2011). This capacity of formation of secondary metabolites is exemplified by production of geosmin, the compound responsible for the odour of tilled soil (Kieser et al 2000), and of biosurfactant molecules, which are surface active agents synthesized by microbial cells (Gandhimathi et al 2009).…”

Section: Introductionmentioning

confidence: 99%

Actinobacteria occurrence and their metabolic characteristics in the nickel-contaminated soil sample

et al. 2014

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Heavy metals are a significant source of pollution in soils that have been demonstrated to exert significant toxic effect on soil microbial assemblages. Here we investigate the occurrence and metabolic characteristics of actinobacteria, which form a predominated component of farmland bacterial community near the town of Sereď in southwest Slovakia, contaminated by close nickel ore facility. Actinobacteria occurred in this environment with high concentrations of nickel (2.109 mg/kg), slightly above the natural occurrence of cobalt (355 mg/kg) and zinc (177 mg/kg), even too low concentration of iron (35.75 mg/kg) for a normal soil and not a toxic amount of copper (32.2 mg/kg) and cadmium (<0.25 mg/kg). The phylogeny was reconstructed using partial sequences of 16S rDNA genes of both, actinobacterial isolates and clones. A total of 105 actinobacterial representatives were divided into 66 species belonging to one order, 7 genera and 5 uncategorized groups. The selected 14 morphologically distinct isolates were able to produce drop collapsing, haemolytic and lipase activities. Whereas only 4 isolates produced dark brown melanin pigment and only 5 of them produced decolourization of the azo dye, all isolates tested were capable of assimilating all 11 sugars tested. All these actinobacterial isolates were resistant to nickel, cobalt, zinc, cadmium, copper, but the level of resistance differed between the individual isolates, and the resistance profiles of antibiotics (gentamycin, ampicillin, ciprofloxacin, chloramphenicol, erythromycin, rifampicin, penicillin-G) varied among them to a certain extent. Our results suggested that actinobacteria in soil contaminated by nickel present a relatively divergent group inside of microbial assemblage.

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Actinomycete Enzymes

Cited by 66 publications

References 253 publications

Cloning and Expression of an Intracellular Alkaline Protease Gene from AlkalopihilicThermoactinomycessp. Η8682

Cloning and Expression of an Intracellular Alkaline Protease Gene from AlkalopihilicThermoactinomycessp. Η8682

Trypsin-like protease of Streptomyces exfoliatus SMF13, a potential agent in mycelial differentiation

Actinobacteria occurrence and their metabolic characteristics in the nickel-contaminated soil sample

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