Isolation and characterization of the gene encoding a novel, thermostable serine proteinase from the mould <i>Tritirachium album</i> Limber

Samal, Babru; Karan, Barbara; Boone, Thomas C.; Osslund, Timothy D.; Chen, K. K.; Stabinsky, Y.

doi:10.1111/j.1365-2958.1990.tb00558.x

Cited by 20 publications

(4 citation statements)

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“…Tritirachium species have been described as airborne contaminants and have been isolated from plant and packing material [ 25 ] and from soil [ 26 , 27 ]. T. album limber is a producer of serine protease [ 27 , 28 ]. Although not common in the marine environment, T. candoliense has also been isolated from the anoxic zone in the Arabian Sea [ 29 ] and others have been isolated from Australian coastal waters [ 30 ].…”

Section: Resultsmentioning

confidence: 99%

Growth of marine fungi on polymeric substrates

et al. 2016

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BackgroundMarine fungi are a diverse group of opportunistic and obligate organisms isolated from marine environments. These fungi are now often included in screens for novel metabolites, while less attention has been given to their production of hydrolytic enzymes. Most enzymes derived from marine microorganisms have been obtained from marine bacteria. The enzymes produced by marine fungi may have different properties than those derived from bacteria or from terrestrial fungi. Here we assess the growth of six filamentous marine fungi on a wide range of polymeric substrates as an indication of their general capacity to produce hydrolytic enzymes.ResultsCalcarisporium sp. KF525, Tritirachium sp. LF562, Bartalinia robillardoides LF550, Penicillium pinophilum LF458, Scopulariopsis brevicaulis LF580 and Pestalotiopsis sp. KF079 all grew on both casein and gelatin as N-source, indicating secretion of proteases. All species also grew on starch, laminarin, xylan, pectin and oil, indicating production of amylases, glucanases, xylanases, pectinases and lipases. Growth on cellulose occurred but was weaker than on xylan. All strains also grew to some extent on sulphated arabinogalactan, although only LF562 could utilise arabinose. Four strains grew on the sulphated ulvans, whereas only KF525 grew on agar or carrageenan. KF525 and LF562 showed limited growth on alginate. Although fucose was used as carbon source by several species, fucoidan did not support biomass production.ConclusionsMarine fungi could be excellent sources of a wide range of hydrolytic enzymes, including those able to hydrolyse various seaweed polymers. Although the native hosts may secrete only small amounts of these enzymes, the genes may provide a rich source of novel enzymes.Electronic supplementary materialThe online version of this article (doi:10.1186/s12896-016-0233-5) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 99%

Growth of marine fungi on polymeric substrates

et al. 2016

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“…The putative mature protein (residues 109-387) is 279aa in length with a calculated molecular mass of 29 kDa. The deduced protein exhibited 96.0, 84.0, 62.3, 62.0, 59.8, 58.6 and 49.3% sequence identity, respectively, to proteinase R of Tritirarchium album (Samal et al 1990); proteinase K of Tritirarchium album (Gunkel and Gassen 1989); alkaline protease of Fusarium (Morita et al 1994); Pr1 of Beauveria brongniartii (Sheng et al 2006); bsn1 of Beauveria bassiana (Joshi et al 1995); pr1 of Metarhizium anisopliae (St. Leger et al 1992) and pr1B of Metarhizium anisopliae (Joshi et al 1997). A dendrogram was created from the sequence alignment of various members of serine peptidase family S8 (Fig.…”

Section: The Deduced Aminoacid Sequence Of Eapmentioning

confidence: 99%

Molecular cloning and homology modelling of a subtilisin-like serine protease from the marine fungus, Engyodontium album BTMFS10

Corso

Chellappan

Sukumaran

et al. 2010

World J Microbiol Biotechnol

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An alkaline protease gene (Eap) was isolated for the first time from a marine fungus, Engyodontium album. Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular protease that belongs to the subtilase family of serine protease (Family S8). A comparative homology model of the Engyodontium album protease (EAP) was developed using the crystal structure of proteinase K. The model revealed that EAP has broad substrate specificity similar to Proteinase K with preference for bulky hydrophobic residues at P1 and P4. Also, EAP is suggested to have two disulfide bonds and more than two Ca 2? binding sites in its 3D structure; both of which are assumed to contribute to the thermostable nature of the protein.Keywords Engyodontium album Á Alkaline serine protease Á Subtilases Á Homology modelling Abbreviations E. album Engyodontium album EAPEngyodontium album protease (deduced protein) Eap Engyodontium album protease (gene)

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“…However, the proteinases secreted by Rhizopus spp., Candida spp. (best studied in C. albicans) (Monod et al, 1994) and Tritirachium album (Samai et al, 1989, 1990) are the products of multigene families.…”

Section: Introductionmentioning

confidence: 99%

The Rhizopus oryzae secreted aspartic proteinase gene family: an analysis of gene expression

Farley

Sullivan

1998

Microbiology

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Rhizopus oryzae was shown to possess a secreted aspartic proteinase gene family (sap) of at least four members (sapl-sap4). Within the family there was 77-87% identity at the nucleotide level and 7&92% identity at the amino acid level. Transcription of three members of this gene family (sapl-sap3) required an acidic medium (pH ~4 . 5 ) and either nitrogen or sulphur derepression. Regulation was co-ordinate and hierarchical, with pH occupying the higher position in the hierarchy. Exogenous protein increased transcript levels, probably via the provision of metabolic intermediates rather than by direct induction of gene expression. sap4 was not expressed under these conditions. SAP1-SAP4 are predicted to have almost identical substrate-binding sites and therefore substrate specificity. It is proposed that sapl-sap3 exist to provide amplified expression of the secreted aspartic proteinase because protein, an important secondary nitrogen source for this fungus, requires extensive degradation to make its nitrogen available to the cell.

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Isolation and characterization of the gene encoding a novel, thermostable serine proteinase from the mould Tritirachium album Limber

Cited by 20 publications

References 21 publications

Growth of marine fungi on polymeric substrates

Growth of marine fungi on polymeric substrates

Molecular cloning and homology modelling of a subtilisin-like serine protease from the marine fungus, Engyodontium album BTMFS10

The Rhizopus oryzae secreted aspartic proteinase gene family: an analysis of gene expression

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