Two new extracellular serine proteases from Streptomyces fradiae

Sinha, Uma; Wolz, Sarah A.; Lad, Pushkaraj J.

doi:10.1016/0020-711x(91)90133-8

Cited by 21 publications

(11 citation statements)

References 11 publications

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“…Research indicated that certain strains of S. fradiae can often act as a producer of multiple proteolytic enzymes (Nickerson et al 1963;Morihara et al 1967;Sinha et al 1991). Likely, striking keratinase activity was also observed by extensive hydrolysis of feather and human hair with the strain S. fradiae var.k11 stored in our laboratory.…”

Section: Discussionmentioning

confidence: 72%

“…Serine proteases (Chandrasekaran and Dhar 1987;Kitadokoro et al 1994;Yum et al 1994;Taguchi et al 1995) and other proteases have been purified and characterized in Streptomycetes. Some serine proteases derived from Streptomycetes (Sinha et al 1991;Moormann et al 1993;Böckle et al 1995;Suzuki et al 1997;Bressollier et al 1999) or other microorganisms (Takiuchi et al 1984;Lin et al 1992;Kulakova et al 1999) were identified as keratinolytic proteases. Keratinases could be very useful in industrial applications, e.g., hydrolysis of high molecular mass substrates such as feather, hair, and leather to produce amino acids or peptides (Papadopoulos 1989;Dalev and Neitchev 1991).…”

Section: Introductionmentioning

confidence: 96%

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Gene cloning and heterologous expression of a serine protease fromStreptomyces fradiaevar.k11

Meng

Cao

et al. 2007

Can. J. Microbiol.

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The gene sfp1, which encodes a predicted serine proteinase designated SFP1, was isolated by the screening of a gene library of the feather-degrading strain Streptomyces fradiae var.k11. The open reading frame of sfp1 encodes a protein of 454 amino acids with a calculated molecular mass of 46.19 kDa. Sequence analysis reveals that SFP1 possesses a typical pre-pro-mature organization that consists of a signal sequence, an N-terminal propeptide region, and a mature proteinase domain. The pre-enzyme of SFP1 was expressed in Escherichia coli and consequently purified. The 25.6 kDa fraction with protease activity separated by gel filtration chromatography indicated that the mature enzyme of SFP1 was formed by autolysis of the propeptide after its expression. The purified SFP1 is active under a broad range of pH and temperature. SFP1 has pH and temperature optima of pH 8.5 and 65 degrees C for its caseinolytic activity and pH 9 and 62 degrees C for its keratinolytic activity. SFP1 was sharply inhibited by the serine proteinase inhibitor phenylmethyl sulfonyl fluoride and exhibited a good stability to solvents, detergents, and salts. Comparison of the protease activity of SFP1 with other commercial proteases indicates that SFP1 has a considerable caseinolytic and keratinolytic activity as does proteinase K.

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Section: Discussionmentioning

confidence: 72%

Section: Introductionmentioning

confidence: 96%

Gene cloning and heterologous expression of a serine protease fromStreptomyces fradiaevar.k11

Meng

Cao

et al. 2007

Can. J. Microbiol.

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“…Since two disulfide bridges in SGPA and SGPB are formed between Cysl5 and Cys36 and between Cysl41 and Cys167 [6], the disulfide bridges of SFase-2 may be formed in a similar manner. Furthermore, SFase-2 has 90% similarity in the N-terminal sequence of 20 residues with a 17.6-kDa chymotrypsin-like proteinase reported by Sinha et al [26]. Sinha et al did not determine the complete amino acid sequence of their proteinase, but since they produced it from the same strain of Streptomyces as SFase-2, after determining its primary structure, much sequence similarity can be expected.…”

Section: Partial Nucleotide Sequence Of the Sfase-2 Genementioning

confidence: 97%

“…This value agreed well with that of 19002 kDa calculated from the amino acid sequence, which is described below. Sinha et al reported that S. frudiae produced two serine proteinases which have molecular masses of 17.6 kDa and 24 kDa [26]. Judging 22 -251. from the difference in the molecular mass, SFase-2 may differ from these two enzymes.…”

Section: Characterization Of Sfase-2mentioning

confidence: 99%

Purification, characterization, primary structure, crystallization and preliminary crystallographic study of a serine proteinase from Streptomyces fradiae ATCC 14544

Kitadokoro

Tsuzuki

Nakamura

et al. 1994

European Journal of Biochemistry

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A proteinase having wide substrate specificity was isolated from Streptomyces fradiae ATCC 14544. This proteinase, which we propose to call SFase-2, was purified from the culture filtrate by S-Sepharose chromatography. The purified enzyme showed an apparent molecular mass of 19 kDa on SDSPAGE. When synthetic peptides were used as substrates, SFase-2 showed broad substrate specificity. It also hydrolyzed keratin, elastin and collagen as proteinaceous substrates. It was completely inhibited by diisopropylfluorophosphate and chymostatin, but not by tosylphenylalaninechloromethane, tosyllysinechloromethane or EDTA, indicating that it can be classified as a serine proteinase.The matured protein sequence of SFase-2 was determined by a combination of amino acid sequencing and the DNA sequencing of the gene. For insight into the three-dimensional structure of SFase-2, we obtained single crystals by the vapor diffusion method using sodium phosphate as a precipitant. These crystals belonged to the orthorhombic, space group P2,2,2, with cell dimensions a = 6.92 nm, b = 7.28 nm, c = 2.99 nm; one molecule was present in the asymmetric unit.Many studies have been done with the serine proteinases produced by Streptomycetes. Streptomyces griseus, in particular, produces many proteinases [l, 21, three of which have been well studied: proteinase A (SGPA) [3], proteinase B (SGPB) [4], and trypsin-like proteinase [5]. These enzymes have been isolated from the commercially available extracellular filtrate, termed Pronase (Kaken Seiyaku, Tokyo) ; their primary structures, biochemical properties and X-ray structures have been reported [6-81. Recently, an acidic-aminoacid-specific proteinase from S. griseus has been described [9, 101. The serine proteinases produced by S. fradiae have been described by Morihara et al. 1111 and Nickerson et al. [12].

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“…Moreover, Bacillus strains are thermophile microorganisms and this property can be used in controlled process for efficient and fast degeneration of feathers. Other bacterial strains known by their keratinolytic activity include B. pumilis , Streptomyces pactum (Bokle et al, 1995) and Streptomyces fradiae (Kunert, 1989;Sinha et al, 1991), Bacillus spp. (Kao Ming-Muh and Hsing-Yao, 1995).…”

Section: Resultsmentioning

confidence: 99%

Feather wastes digestion by new isolated strains Bacillus sp. in Morocco

Zerdani¹,

Faïd²,

Malki³

2004

Afr. J. Biotechnol.

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Eight strains of Bacillus were isolated from non treated soil, characterized and used for the digestion of feather wastes in the laboratory. Non-protein nitrogen (NPN) and total protein (TP) were determined during the incubation time and the microbial counts of the different strains during feather hydrolysis were also monitored. Results of the screening test showed that the solid pieces of feather were completely digested by all the strains. The most efficient isolated strain selected was compared with Bacillus subtilis ATCC 6633. Results showed that the total protein decreased from 13.6% to 1.92 % with the isolated strain, and from 12.25 % to 2.99% with the standard strain. The NPN reached a concentration of 43.2mg/100g and 20.5 mg/100g with the isolated and standard strains, respectively.

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Two new extracellular serine proteases from Streptomyces fradiae

Cited by 21 publications

References 11 publications

Gene cloning and heterologous expression of a serine protease fromStreptomyces fradiaevar.k11

Gene cloning and heterologous expression of a serine protease fromStreptomyces fradiaevar.k11

Purification, characterization, primary structure, crystallization and preliminary crystallographic study of a serine proteinase from Streptomyces fradiae ATCC 14544

Feather wastes digestion by new isolated strains Bacillus sp. in Morocco

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