Purification and Properties of<i>Bacillus acidopullulyticus</i>Pullulanase

Kusano, Shuichi; Nagahata, Naokazu; Takahashi, Shinichiro; Fujimoto, Daisaburo; Sakano, Yuji

doi:10.1080/00021369.1988.10869024

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“…KSM-1876 generates maltotriose, and not panose and isopanose from pullulan. Unlike pullulanases from Bacillus 25 ) and isoamylases from Pseudomonas 26 ) and potato, 2 7) our pullulanase, as well as the enzyme from Klebsiella pneumoniae, 1) is unique in that it cannot hydrolyze glycogens from oyster and rabbit liver. The alkaline pullulanase from Bacillus strain no.…”

Section: Discussionmentioning

confidence: 99%

Purification and Some Properties of an Alkaline Pullulanase from AlkalophilicBacillussp. KSM-1876

Ara

Igarashi

Saeki

et al. 1992

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionmentioning

confidence: 99%

Purification and Some Properties of an Alkaline Pullulanase from AlkalophilicBacillussp. KSM-1876

Ara

Igarashi

Saeki

et al. 1992

Bioscience, Biotechnology, and Biochemistry

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Heat-stable pullulanase from Bacillus acidopullulyticus : characterization and refolding after guanidinium chloride-induced unfolding

et al. 1999

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Heat-stable pullulanase from Bacillus acidopullulyticus was characterized with respect to its stability against thermal and chemical denaturation and its reactivation after complete chemical unfolding. The enzyme was quite thermostable and retained 55% of activity after heating at 60 degrees C for 30 min at pH 5.5. At pH 6.0, only 9% residual activity was observed. The addition of sucrose, polyols, and Na2SO4 strongly stabilized the enzyme against thermal inactivation. The processes of chemical unfolding by guanidinium chloride (GdmCl) and refolding were studied by enzymological and spectroscopic criteria. B. acidopullulyticus pullulanase was very sensitive to GdmC1 denaturation and had a transition midpoint at 1.2M GdmCl. Reactivation after complete unfolding in 5 M GdmCl was initiated by dilution of the unfolding mixture: 67% reactivation was observed under standard conditions. The influence of some chemical and physical parameters (pH, chemical agents, temperature, and unfolding and refolding time) on refolding was investigated. Of the additives tested to assist reactivation, only bovine serum albumin (BSA) increased the yield of activity to 80%. The full regain of structure and activity was proven by comparing the enzymological, physicochemical, and spectroscopic properties of the native and refolded pullulanase.

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Purification and Properties ofBacillus acidopullulyticusPullulanase

Cited by 2 publications

References 1 publication

Purification and Some Properties of an Alkaline Pullulanase from AlkalophilicBacillussp. KSM-1876

Purification and Some Properties of an Alkaline Pullulanase from AlkalophilicBacillussp. KSM-1876

Heat-stable pullulanase from Bacillus acidopullulyticus : characterization and refolding after guanidinium chloride-induced unfolding

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