Deep-sea fungi as a source of alkaline and cold-tolerant proteases

Damare, Samir; Raghukumar, Chandralata; Muraleedharan, Usha Devi; Raghukumar, Seshagiri

doi:10.1016/j.enzmictec.2006.03.032

Cited by 74 publications

(27 citation statements)

References 24 publications

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“…These findings were very similar to that of Anandan et al (2007) who also reported that Hg 2+ was strong inhibitor of alkaline protease activity while Ca 2+ and Mg 2+ had slight effect on enzyme activation. Some studies reported that Zn 2+ acted as inhibitor for cysteine proteases (Damare et al 2006;Gaur et al 2008). …”

Section: Effect Of Metalsmentioning

confidence: 99%

Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae

Mushtaq

Irfan

Nadeem

et al. 2015

Braz. arch. biol. technol.

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Section: Effect Of Metalsmentioning

confidence: 99%

Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae

Mushtaq

Irfan

Nadeem

et al. 2015

Braz. arch. biol. technol.

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“…Marine microorganisms are emerging as a potential source of alkaline serine proteases and there are few reports on the extraction of alkaline serine protease from marine microbes with novel attributes like thermostability, salt tolerance and solvent stability (Makino et al 1981;Manachini and Fortina 1998;Estrade-Badillo et al 2003;Venugopal and Saramma 2006;Damare et al 2006;Bhaskar et al 2007). Earlier, we had reported the production of an extracellular serine protease from an alkaliphilic and salt tolerant marine fungus, Engyodontium album which was characterized for its physiochemical and biochemical properties (Chellappan et al 2006).…”

Section: Introductionmentioning

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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“…Proteases originating from plants (papain, bromeline) and animals (trypsin, chemotrypsin, pepsin, rennin) are well-known and thoroughly examined [47]. Microorganisms are the most attractive sources of proteolytic enzymes, hardly limited by scale of production.Proteolytic enzymes are synthesized by various microbial culturesbacteria, yeasts, streptomycetes, fungi [7,12,20,37,40,47]. Bacteria of genera Bacillus, Lactobacillus, Fervidobacterium, Pseudomonas, Microbacterium, Yersinia are recognized as producers of serine, cysteine and metal proteases, aminopeptidases [20,47].…”

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confidence: 99%

Proteolytic Enzymes of Mycelial Fungi

Михайлова

2011

Microbiology&Biotechnology

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Proteolytic enzymes affiliated to hydrolases catalyze reaction of protein hydrolysis to peptides or free amino acids. Proteases are involved in the normal physiological processes of protein and cellular peptide biogenesis in the living species and in abnormal pathological processes. They can be applied in diverse industries, medicine, agriculture and are indispensable as research tools. Proteases originating from plants (papain, bromeline) and animals (trypsin, chemotrypsin, pepsin, rennin) are well-known and thoroughly examined [47]. Microorganisms are the most attractive sources of proteolytic enzymes, hardly limited by scale of production.Proteolytic enzymes are synthesized by various microbial culturesbacteria, yeasts, streptomycetes, fungi [7,12,20,37,40,47]. Bacteria of genera Bacillus, Lactobacillus, Fervidobacterium, Pseudomonas, Microbacterium, Yersinia are recognized as producers of serine, cysteine and metal proteases, aminopeptidases [20,47]. Bacteria of genus Bacillus are applied for industrial production of neutral and alkaline proteases. Representatives of genera Candida and Trichophyton synthesize aspartyl proteases, aminopeptidases, carboxypeptidases, dipeptidylpeptidases, Streptomyces -serine proteases [7,37].Mycelial fungi are the most promising cultures for large-scale manufacturing of proteolytic enzymes. They synthesize extracellular proteases belonging to various families and subfamilies, showing activity

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Deep-sea fungi as a source of alkaline and cold-tolerant proteases

Cited by 74 publications

References 24 publications

Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae

Kinetics Study of Extracellular Detergent Stable Alkaline Protease from Rhizopus oryzae

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

Proteolytic Enzymes of Mycelial Fungi

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