Molecular cloning and comparative sequence analysis of fungal β-Xylosidases

Mustafa, Ghulam; Kousar, Sumaira; Rajoka, Muhammad Ibrahim; Jamil, Amer

doi:10.1186/s13568-016-0202-3

AMB Express

Table 1 Cloning of different bacterial β-Xylosidase genes in E. coli

From: Molecular cloning and comparative sequence analysis of fungal β-Xylosidases

Source organism	Gene	Vector	Host	Molecular mass of the recombinant enzyme (kDa)	Characteristics of the recombinant enzyme	Reference
C. stercorarium F-9	Xyl43B	pYK306, pT7Blue T, pET-28a	E. coli JM109, E. coli DH5α	56.3	Temperature = 80 °C pH 3.5 enzyme activity = 10 U mg^− 1stability 15 min at 50–70 °C K_m = 6.2 mm V_max = 15 μmol min⁻¹ mg⁻¹	Suryani et al. (2004)
C. stercorarium F-9		pBR322	E. coli JM109	–	Temperature = 80 °C enzyme activity = 8.16 U mg⁻¹	Sakka et al. (1990)
Butyrivibrio fibrisolvens GS113	xylB	pUC18	E. coli DH5α	60	Specific activity 0.2 nmol min⁻¹ mg⁻¹	Utt et al. (1991)
B. stearothermophilus 21	xylA	pUC19	E. coli JM109	75	Enzyme activity 1.56 U 10 mL⁻¹	Baba et al. (1994)
Thermoanaerobacterium sp. JW/SL YS485	xylB	pUC18	E. coli TG-1	58.5	Temperature = 65 °C pH = 6.0 specific activity = 0.53 U mg⁻¹	Lorenz and Wiegel (1997)
Thermotoga thermarum DSM 5069	XynB3	pET-20b	E. coli Top10 and BL21 (DE3)	85 kD	Temperature = 95 °C pH 6.0 specific activity = 116 U mg ⁻¹Km = 0.27 mM V_max = 223.2 U mg⁻ ¹ K_cat/K_m 1173.4 mM⁻¹ s⁻¹	Shi et al. (2013)
P. ruminicola B₁4	xynB	pUC19/L3	E. coli DH 5α	–	pH = 6.5 enzyme activity = 540 nmol min⁻¹ mg⁻¹	Gasparic et al. (1995)
C. saccharolyticum Tp8T6.3.3.1	aryl	pBR322	E.coli	53	Temperature = 70 °C pH = 5.7 specific activity = 49.2 µmol min⁻¹ mg^−1 km = 10 mM V_max = 64 U mg⁻¹	Hudson et al. (1991)
Bifidobacterium breve K-110	XylBK	pGEM-T	E. coli BL21(DE3) JM109(DE3)	55.7	Temperature = 45 °C pH = 6.0 specific activity = 3.32 Umg^−1 km = 1.45 mM V_max = 10.75 μmol min⁻¹ mg⁻¹	Hyun et al. (2012)
Thermobifida fusca	Xyl43A	pIJ702	E. coli BL21(DE3)/pLysS	–	Temperature = 55–60 °C pH = 5.5–6.0 km = 0.23 mM K_cat = 4.83 s⁻¹	Morais et al. (2011)
Ruminococcus albus 8	Xyl3A	pET-46b	E. coli JM109	77.3		Moon et al. (2011)
S. thermoviolaceus OPC-520	bxlA	pUC18 pUC19	E. coli JM109	82	Optimum temperature = 50 °C optimum pH = 6.5 stable at 50 °C activity lost at 60 °C	Tsujibo et al. (2001)
Thermoanaerobacterium saccharolyticum B6A-RI	xynB	pHC79 (BRL)	E. coli DH5a	60	Optimum temperature = 65 °C loss of activity at 85 °C half-life = 55 min at 75 °C	Lee and Zeikus (1993)
Thermoanaerobacterium saccharolyticum JW/SL-YS485	XylC	pMD19-T	E. coli JM109	78	Temperature = 65 °C pH = 6.0 specific activity = 45.8 U mg⁻¹ half-life = 1 h at 67 °C K_m = 28 mM V_max = 276 U mg⁻¹	Shao et al. ( 2011)
P. woosongensis KCTC 3953 (DSM 16971)	XylC	pUC19 pET23a(+)	E. coli DH5α E. coli BL21(DE3)	55	Temperature = 95 °C pH = 6.5 specific activity = 659.9 mU mg−1 protein K_m = 8.5 mM V_max = 3.1 µmol min⁻¹mg⁻¹ half-life = 22 min at 95 °C	Kim and Yoon (2010)
Butyrivibrio fibrisolvens GS113	xylB	pUC18	E. coli DHS5α	60	Temperature = 60 °C pH = 5.5 specific activity = 0.13 µmol min⁻¹ mg⁻¹	Sewell et al. (1989)
B. halodurans C-125	Bxyl	pQEBxyl	E coli JM109	61	Temperature = 45 °C pH = 7.0 enzyme activity = 7811.1 mU K_m = 1.9 mmol L⁻¹ V_max = 0.65 µmol min⁻¹ mg⁻¹	Liang et al. (2009)
Vibrio sp. XY-214	xloA	pBluescriptII KS (−)	E. coli DH5α	60	Temperautre = 35 °C pH = 7.0 km = 0.244 mM V_max = 1.82 µmol min-1 mg⁻¹	Umemoto et al. (2008)

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