Biodegradation of starch and α-glycan polymers

Ramesh, M.; Saha, Badal C.; Mathupala, Saroj P.; Podkovyrov, S M; Zeikus, J. G.

doi:10.1007/978-94-011-1687-9_10

Cited by 2 publications

(2 citation statements)

References 118 publications

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“…Root exudates also contribute significantly to the water-soluble pool of rapidly metabolized organic materials. Simple sugars and free amino acids can directly be transported into the cell and undergo glycolysis and then enter the appropriate metabolic pathway (Ramsh et al, 1994;Wagner and Wolf, 1999). Depending on microbial species, disaccharides can be transported directly into the cell to undergo hydrolysis or the molecule can be hydrolyzed outside the cell and then transported (Griffin, 1994).…”

Section: Catabolismmentioning

confidence: 99%

Biogeochemistry of Decomposition and Detrital Processing

Sanderman¹,

Amundson²

2014

Treatise on Geochemistry

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Section: Catabolismmentioning

confidence: 99%

Biogeochemistry of Decomposition and Detrital Processing

Sanderman¹,

Amundson²

2014

Treatise on Geochemistry

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“…Amylopullulanase can be further divided into two subgroups based on the number of active sites within the protein [6]. Most amylopullulanases from thermophilic anaerobes possess one active site [7–10]. On the other hand, amylopullulanases from aerobic micro‐organisms contain either one [11,12] or two active sites [13,14].…”

Section: Introductionmentioning

confidence: 99%

Structure and expression of an amylopullulanase gene from Bacillus stearothermophilus TS‐23

Chen

et al. 2001

Biotech and App Biochem

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An amylopullulanase gene (apuTS) from Bacillus stearothermophilus TS-23 was cloned and characterized. apuTS consisted of an open reading frame of 6054 bp encoding a protein of 2018 amino acids with a calculated M(r) of 223811. The deduced amino acid sequence revealed four highly conserved regions that are common among amylolytic enzymes. In the C-terminal region, a six-amino-acid sequence (Pro-Gly-Ser-Gly-Thr-Thr) is repeated nine times. It shared the highest degree of homology with the amylopullulanase of Bacillus sp. XAL601. The enzyme also had moderate homology with amylopullulanases from thermophilic anaerobic bacteria. Low levels of homology were observed between the ApuTS of B. stearothermophilus TS-23 and amylopullulanases of Pyrococcus abyssi Orsay, P. furiosus and Bacillus sp. KSM1378. When the intact coding region of apuTS was expressed in Escherichia coli under the control of the lac promoter, the product was degenerate, as revealed by amylase activity staining after SDS/PAGE. The largest active polypeptide had an M(r) of about 220000, while the smallest one had an M(r) of about 105000. Upstream of the apuTS gene, a gene orfX was fortuitously cloned. The putative OrfX protein was weakly related to the myosin heavy chain. It was predicted to contain a central, 179-residue-long, coiled-coil domain.

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Biodegradation of starch and α-glycan polymers

Cited by 2 publications

References 118 publications

Biogeochemistry of Decomposition and Detrital Processing

Biogeochemistry of Decomposition and Detrital Processing

Structure and expression of an amylopullulanase gene from Bacillus stearothermophilus TS‐23

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