Isolation and partial characterization of an extracellular protease from <i>Sporotrichum dimorphosporum</i>

Tapia, Guillermina; Curotto, E.; O'Reilly, Sybil; González, Gustavo

doi:10.1016/0014-5793(81)81120-9

Cited by 10 publications

(3 citation statements)

References 11 publications

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“…In order to better clarify the relationship between laccases and proteases in P. ostreatus and the role of these extracellular proteases, we have purified and characterized a protease (PoSl) from the fungal culture broth. PoSl is a monomeric glycoprotein with a molecular mass of 75 kDa, which is larger than that determined for most fungal proteases (5,7,9,15,19,22).…”

Section: Discussionmentioning

confidence: 82%

Purification, Characterization, and Functional Role of a Novel Extracellular Protease from Pleurotus ostreatus

Palmieri¹,

Bianco

Cennamo

et al. 2001

Appl Environ Microbiol

124

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A new extracellular protease (PoSl; Pleurotus ostreatus subtilisin-like protease) from P. ostreatus culture broth has been purified and characterized. PoSl is a monomeric glycoprotein with a molecular mass of 75 kDa, a pI of 4.5, and an optimum pH in the alkaline range. The inhibitory profile indicates that PoSl is a serine protease. The N-terminal and three tryptic peptide sequences of PoSl have been determined. The homology of one internal peptide with conserved sequence around the Asp residue of the catalytic triad in the subtilase family suggests that PoSl is a subtilisin-like protease. This hypothesis is further supported by the finding that PoSl hydrolysis sites of the insulin B chain match those of subtilisin. PoSl activity is positively affected by calcium. A 10-fold decrease in the K m value in the presence of calcium ions can reflect an induced structural change in the substrate recognition site region. Furthermore, Ca 2؉ binding slows PoSl autolysis, triggering the protein to form a more compact structure. These effects have already been observed for subtilisin and other serine proteases. Moreover, PoSl protease seems to play a key role in the regulation of P. ostreatus laccase activity by degrading and/or activating different isoenzymes.White rot basidiomycetes have received extensive attention because of their lignin-degrading activity. The biochemistry of lignin degradation is a complex process involving a series of enzymatic and nonenzymatic reactions. Extracellular enzymes which catalyze oxidative reactions are lignin peroxidases, laccases, manganese peroxidases, and hydrogen peroxide-producing enzymes (3, 13). Even though their catalyzed reactions have been studied in detail, their in vivo coordination and, possibly, synergistic action are not clearly understood.Pleurotus ostreatus is a white rot basidiomycete which belongs to the subclass of ligninolytic microorganisms that produce laccases, manganese peroxidases, and veratryl alcohol oxidases but no lignin peroxidase. Among these enzymes, laccases have been the most widely studied and characterized (11,12,17). In a recent study (16), it has been demonstrated that a laccase isoenzyme (POXA1b; phenol oxidase A1b) is specifically degraded in the early phase of fungal growth by proteases present in P. ostreatus culture broth; hence, the disappearance of POXA1b seems to be correlated with the appearance of extracellular protease activity. A similar relationship was observed for lignin peroxidases in Phanerochaete chrysosporium, and, in this case, the extracellular proteases caused an almost complete disappearance of lignin peroxidase activity due to degradation of all lignin peroxidase isoenzymes (8). Furthermore, a recent report (21) suggests that both intracellular and extracellular proteases are involved in the regulation of ligninolytic activities in cultures of Trametes versicolor under nutrient limitation. In contrast, it has been reported (2) that proteases are not responsible for the decrease in peroxidase activity in Pleurotus pulmonarius ...

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Section: Discussionmentioning

confidence: 82%

Purification, Characterization, and Functional Role of a Novel Extracellular Protease from Pleurotus ostreatus

Palmieri¹,

Bianco

Cennamo

et al. 2001

Appl Environ Microbiol

124

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“…Recently, extracellular proteinases from other basidiomycetes have also been reported to be S-PI insensitive (240). An extracellular proteinase from the basidiomycete Sporotrichum dimorphosporum has recently been described, but its sensitivity to inhibitors was not reported (328). An examination of the specificity of proteinases Al and A2 of S. lignicolum suggests that the nature of the amino acid at the P'1 position (as defined by Schechter and Berger [286]) is less important than in the other acid proteinases, in which a bulky amino acid is preferred (208).…”

Section: Aspartic Proteinasesmentioning

confidence: 99%

Comparative biochemistry of the proteinases of eucaryotic microorganisms.

North¹

1982

Microbiological Reviews

196

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“… Aspartato proteasas (EC 3.4.23): También son conocidas como proteasas ácidas, debido a la presencia de uno o dos grupos carboxilos que contiene en el centro activo; son inhibidas por pepstatina, acetil pepstatinay epóxidos. La gran mayoría de las enzimas pertenecientes a esta clasificación son activas a valores de pH ácidos.En hongos microoscópicos, la gran mayoría de estas enzimas presenta pI por debajo de pH 5.1 (entre 3.4 y 4.6), excepto de las proteasas de Sporotrichumdimorphosporum (pH 7.4) (Tapia et al, 1981).…”

Section: Proteasasunclassified

Estudio de las enzimas fenoloxidasas, proteasas y peroxidasas presentes en Rhizopus oryzae ENHE

Badillo

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II ÍNDICE DE GRÁFICAS Gráfica 1 Crecimiento de R. oryzae ENHE en cuanto a su biomasa seca obtenida de medio Lee sin inductores y pH del medio extracelular sin inductores Gráfica 2 Actividades enzimáticas proteasas ácidas, neutras y alcalinas a nivel extracelular en R. oryzae ENHE Gráfica 3 . Actividad LiP a nivel extracelular en R. oryzae ENHE crecido con y sin alcohol veratrílico en el medio Lee Gráfica 4 Actividades enzimáticas proteasas ácidas, neutras y alcalinas a nivel intracelular en R. oryzae ENHE Gráfica 5 Decoloración de azul de anilina a través del tiempo por parte de la LiP presente en los extractos extracelulares.

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Isolation and partial characterization of an extracellular protease from Sporotrichum dimorphosporum

Cited by 10 publications

References 11 publications

Purification, Characterization, and Functional Role of a Novel Extracellular Protease from Pleurotus ostreatus

Purification, Characterization, and Functional Role of a Novel Extracellular Protease from Pleurotus ostreatus

Comparative biochemistry of the proteinases of eucaryotic microorganisms.

Estudio de las enzimas fenoloxidasas, proteasas y peroxidasas presentes en Rhizopus oryzae ENHE

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