2004
DOI: 10.1016/j.enzmictec.2004.05.004
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Purification and properties of a maltotriose-producing α-amylase from Thermobifida fusca

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Cited by 66 publications
(42 citation statements)
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“…MSC702 which had 2.98 fold purification and a yield of 56.58% by ammonium sulphate precipitation (40-60% saturation), was reported by Singh et al, (2014). Fifty-five percent (55%) recovery of amylase from Thermobifida fusca NTU22 having a purification fold of 1.3 by ammonium sulphate precipitation was reported by Yang and Liu (2004). Purification fold of 1.3 and 4.29% yield of amylase produced by Geobacillus LH8 strain was obtained (Mollania et al, 2010).…”
Section: Effect Of Metal Ions On Partially Purified Amylase Activitymentioning
confidence: 97%
“…MSC702 which had 2.98 fold purification and a yield of 56.58% by ammonium sulphate precipitation (40-60% saturation), was reported by Singh et al, (2014). Fifty-five percent (55%) recovery of amylase from Thermobifida fusca NTU22 having a purification fold of 1.3 by ammonium sulphate precipitation was reported by Yang and Liu (2004). Purification fold of 1.3 and 4.29% yield of amylase produced by Geobacillus LH8 strain was obtained (Mollania et al, 2010).…”
Section: Effect Of Metal Ions On Partially Purified Amylase Activitymentioning
confidence: 97%
“…Продуценти α-амілаз виявлено і се-ред актиноміцетів (Nocardiopsis [29], Nocardia [1], Streptomyces [1], Thermomonospora [11,30], Thermobifida [31], Thermoactinomyces [11,30,32,33]) та дріжджів (Cryptococcus [34], Saccharomycopsis [35]). …”
Section: джерела мікробних α-амілазunclassified
“…Для більшості α-амілаз, виділених з бактерій і грибів (T. thalpophilus KSV 17, P. citrinum HBF62, A. oryzae, T. fusca, A. niger, A. flavus var. oryzae) [1,22,25,31,32,48,63], оптимальний рівень рН знаходить-ся в слабо кислій та нейтральній області. Хоча деякі α-амілази (B. cohnii US147, A. niger JGI 24) виявляють активність за лужних [21,37] та екстремальних (3,0-4,5) значень рН.…”
Section: фізико-хімічні властивості α-амілазunclassified
“…The eluted enzymatically active fractions were pooled and used for molecular size determination. The active portions were tested by spotting onto starch agar plates and flooding with iodine (Yang and Liu, 2004).…”
Section: Methodsmentioning
confidence: 99%