Purification and preliminary characterization of an extracellular pullulanase from Thermoanaerobium Tok6-B1

Plant, Adrian R.; Clemens, Robyn M.; Daniel, Roy M.; Morgan, Hugh W.

doi:10.1007/bf00253526

Cited by 48 publications

(26 citation statements)

References 26 publications

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“…In general, pullulanase debranches amylopectin, beta-limit dextrins and soluble starch, but cannot act on amylose (Abdullah and French 1970). However, it has been shown that pullulanases from thermophiles such as C. therrnohydrosulfuricum (Melasniemi 1987;Saha et al 1988), Thermoanaerobium brockii (Coleman et al 1987), Thermoanaerobium Tok-B1 (Plant et al 1987) and mesophilic B. subtilis (Takasaki 1987) are different from other described pullulanases. These pullulanases degrade alpha-l,4-glucosidic linkages of starch to produce mixtures of DP2-DP4.…”

Section: Discussionmentioning

confidence: 99%

“…Several new sources of thermostable pullulanases have been reported, mainly in thermoanaerobes (Hyun and Zeikus 1985;Antranikian et al 1987;Coleman et al 1987;Melasniemi 1987;Nakamura et al 1987;Plant et al 1987;. Although mesophilic Bacillus strains can produce pullulanase (Nakamura et al 1975;Adams and Priest 1977;Jensen and Norman 1984), these activities are not thermostable at temperatures higher than 60 ° C. The crude extracellular enzyme preparation of Bacillus strain 3183 contains pullulanase, amylase and saccharidase activities which can hydrolyze soluble starch into a variety of products that may have potential industrial utility.…”

Section: Discussionmentioning

confidence: 99%

“…These pullulanases degrade alpha-l,4-glucosidic linkages of starch to produce mixtures of DP2-DP4. The high starch and pullulan degrading activities in the culture broth of Bacillus strain 3183 suggests that it may have a similar pullulanase activity (Coleman et al 344 1987;Plant et al 1987) a n d / o r a m i x t u r e o f p u l l u l anase, a l p h a -a m y l a s e or a l p h a -g l u c o s i d a s e activities. I n a s e p a r a t e report, we have d e m o n s t r a t e d t h a t an a m y l op u l l u l a n a s e was p u r i f i e d f r o m the c r u d e e n z y m e p r e p aration that d e g r a d e s b o t h a l p h a -l , 4 b o n d s in starch a n d a l p h a -l , 6 b o n d s in p u l l u l a n ( S a h a et al 1989).…”

Section: Discussionmentioning

confidence: 99%

“…Recently, several thermostable pullulanases have been discovered from extreme thermophiles such as Clostridium thermohydrosulfuricum (Hyun and Zeikus 1985;Melasniemi 1987), Thermoanaerobium brockii (Coleman et al 1987), Thermoanaerobium Tok6-B1 (Plant et al 1987), a new Clostridium isolate (Antranikian et al 1987), Thermus aquaticus YT-1 (Plant et al 1986) and Thermus sp. (Nakamura et al 1987).…”

Section: Introductionmentioning

confidence: 99%

“…(Nakamura et al 1987). Some novel pullulanase preparations display the unique property of not only degrading alpha-l,6-glucosidic linkages in pullulan but also degrading the alpha-l,4 linkages of soluble starch, amylose and amylopectin (Coleman et al 1987;Plant et al 1987;. Although Suzuki and Chishiro (1983) and Imanaka and Kuriki (1989) reported that Bacillus stearothermophilus strains produce pullulan hydrolases, the enzymes were not able to cleave alpha-l,6-1inkages of pullulan and were not classified as true pullulanases.…”

Section: Introductionmentioning

confidence: 99%

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Physiological and enzymatic characterization of a novel pullulan-degrading thermophilic Bacillus strain 3183

Shen

Srivastava

Saha

et al. 1990

Appl Microbiol Biotechnol

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A new thermophilic Bacillus strain 3183 (ATCC 49341) was isolated from hot-spring sediments. The organism grew on pullulan as a carbon source and showed optimum pH and temperature at pH 5.5 and 62 ° C, respectively, for growth. The strain reduced nitrate to nitrite both aerobically and anaerobically. It produced extracellular thermostable pullulanase and saccharidase activities which degraded pullulan and starch into maltotriose, maltose, and glucose. Medium growth conditions for pullulanase production were optimized. The optimum pH and temperature for pullulanase activity were at pH 6.0 and 75 ° C, respectively. The enzyme was stable at pH 5.5-7.0 and temperature up to 70 ° C in the absence of substrate. The K,, for pullulan at pH 6.0 and 75°C was 0.4 mg/ml. The pullulanase activity was stimulated and stabilized by Ca 2+. It was inhibited by ethylenediaminetetraacetate (EDTA), betaand gamma-cyclodextrins but not by alpha-cyclodextrin and reagents that inhibit essential enzyme SHgroups.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Physiological and enzymatic characterization of a novel pullulan-degrading thermophilic Bacillus strain 3183

Shen

Srivastava

Saha

et al. 1990

Appl Microbiol Biotechnol

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Pullulan

Leathers¹

2002

Biopolymers Online

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Introduction Historical Outline Chemical Structure Physiological Function Chemical Analyses Occurrence Biosynthesis Culture Conditions and Cell Morphology Biosynthetic Mechanism Genetics and Molecular Biology Biodegradation Production Properties and Applications Patents Outlook and Perspectives

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Natural Polysaccharide‐Degrading Enzymes

Bertoldo¹,

Antranikian²

2002

Enzyme Catalysis in Organic Synthesis

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Starch is the most economically important reserve polysaccharide in the plant kingdom and is in addition the major source of carbohydrates in human nutrition. In contrast to non-starch reserve polysaccharides, which are outside the cell and the plasmalemma, starch is located in the so-called plastids or in vacuoles within the plant cells"]. In seeds, the highest starch content can be found in the endosperm, whereas its content in the embryo and the pericarp is very low. In general, the starch content of seeds or fruits varies with the degree of maturation [']. Starch occurs in semicrystalline form in granules. The size and the shape of the granules is dependent on the plant species and may reach about 175 mm.Starch-degrading enzymes can be divided into two classes according to their reaction mechanism: the glucosidases and the glycosyl-transferases. The first class, the glucosidases, are classified as hydrolases, which catalyze an irreversible hydrolytic cleavage of the glycosidic bond. The group of glucosidases is further subdivided, according their point of attack, into endoacting and exoacting enzymes. Endoacting enzymes hydrolyze linkages in a random manner in the inner part of the starch molecule, releasing linear and branched oligosaccharides with various chain length. a-Amylase is classified as an endoacting enzyme. In contrast to endoacting enzymes,

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Purification and preliminary characterization of an extracellular pullulanase from Thermoanaerobium Tok6-B1

Cited by 48 publications

References 26 publications

Physiological and enzymatic characterization of a novel pullulan-degrading thermophilic Bacillus strain 3183

Physiological and enzymatic characterization of a novel pullulan-degrading thermophilic Bacillus strain 3183

Pullulan

Natural Polysaccharide‐Degrading Enzymes

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