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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제25권 제11호
- 발행연도
- 2015.1
- 수록면
- 1,944 - 1,953 (10page)
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A novel alkaline protease from Streptomyces sp. M30, SapHM, was purified by ammonium sulfate precipitation, hydrophobic interaction chromatography, and DEAE-Sepharose chromatography, with a yield of 15.5% and a specific activity of 29,070 U/mg. Tryptic fragments of the purified SapHM were obtained by electrospray ionization quadrupole timeof- flight mass spectrometry. Nucleotide sequence analysis revealed that the gene sapHM contained 1,179 bp, corresponding to 392 amino acids with conserved Asp156, His187, and Ser339 residues of alkaline protease. The first 24 amino acid residues were predicted to be a signal peptide, and the molecular mass of the mature peptide was 37.1 kDa based on amino acid sequences and mass spectrometry. Pure SapHM was optimally active at 80°C in 50 mM glycine-NaOH buffer (pH 9.0), and was broadly stable at 0-50°C and pH 4.0-9.0. The protease relative activity was increased in the presence of Ni2+, Mn2+, and Cu2+ to 112%, 113%, and 147% of control, respectively. Pure SapHM was also activated by dimethylformamide, dimethyl sulfoxide, Tween 80, and urea. The activity of the purified enzyme was completely inhibited by phenylmethylsulfonyl fluoride, indicating that it is a serine-type protease. The Km and Vmax values were estimated to be 35.7 mg/ml, and 5 × 104 U/mg for casein. Substrate specificity analysis showed that SapH was active on casein, bovine serum albumin, and bovine serum fibrin.
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참고문헌 (23)
참고문헌 신청
Adinarayana K / 2003 / Purification and partial characterization of thermostable serine alkaline protease from a newly isolated Bacillus subtilis PE-11 / AAPS PharmSciTech 4
Amid M / 2014 / Purification and characterization of alkaline-thermostable protease enzyme from pitaya (Hylocereus polyrhizus) waste: a potential low cost of the enzyme / Bio
Anitha TS / 2013 / Purification and characterization of an extracellular keratinolytic protease from a new isolate of Aspergillus parasiticus / Protein Expr. Purif 88 : 214 ~
Banerjee UC / 1999 / Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry detergent additive / Process Biochem 35 : 213 ~ 219
Bessler C / 2007 / Novel alkaline protease from Bacillus gibsonii and washing and cleaning agents containing said novel alkaline protease. Patent appl / WO 2007/131657
Amid M / 2014 / Purification and characterization of alkaline-thermostable protease enzyme from pitaya (Hylocereus polyrhizus) waste: a potential low cost of the enzyme / Bio
Anitha TS / 2013 / Purification and characterization of an extracellular keratinolytic protease from a new isolate of Aspergillus parasiticus / Protein Expr. Purif 88 : 214 ~
Banerjee UC / 1999 / Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry detergent additive / Process Biochem 35 : 213 ~ 219
Bessler C / 2007 / Novel alkaline protease from Bacillus gibsonii and washing and cleaning agents containing said novel alkaline protease. Patent appl / WO 2007/131657
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