Purification and some properties of a novel maltohexaose-producing exo-amylase from Aerobacter aerogenes

Kainuma, Keiji; Wako, Katsuo; Kobayashi, Shôichi; Nogami, Akiko; Suzuki, Shigeo

doi:10.1016/0005-2744(75)90235-1

Cited by 48 publications

(14 citation statements)

References 21 publications

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“…Preincubation of the enzyme (20 min) to determine temperature stability was carried out in the absence of the substrate. It has been shown for other amylases (5,26) that the substrate protects the enzyme against thermal denaturation.…”

Section: Resultsmentioning

confidence: 99%

Cloning, nucleotide sequence, and enzymatic characterization of an alpha-amylase from the ruminal bacterium Butyrivibrio fibrisolvens H17c

et al. 1991

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A Butyrivibrio fibrisolvens amylase gene was cloned and expressed by using its own promoter on the recombinant plasmid pBAMY100 in Escherichia coli. The amylase gene consisted of an open reading frame of 2,931 bp encoding a protein of 976 amino acids with a calculated Mr of 106,964. In E. coli(pBAMY100), more than 86% of the active amylase was located in the periplasm, and TnphoA fusion experiments showed that the enzyme had a functional signal peptide. The B. fibrisolvens amylase is a calcium metalloenzyme, and three conserved putative calcium-binding residues were identified. The amylase showed high sequence homology with other a-amylases in the three highly conserved regions which constitute the active centers. These and other conserved regions were located in the N-terminal half, and no similarity with any other amylase was detected in the remainder of the protein. Deletion of approximately 40% of the C-terminal portion of the amylase did not result in loss of amylolytic activity. The B. fibrisolvens amylase was identified as an endo-oa-amylase by hydrolysis of the Phadebas amylase substrate, hydrolysis of y-cyclodextrin to maltotriose, maltose, and glucose and the characteristic shape of the blue value and reducing sugar curves. Maltotriose was the major initial hydrolysis product from starch, although extended incubation resulted in its hydrolysis to maltose and glucose.Members of the genus Butyrivibrio are among the most numerous and nutritionally versatile of rumen bacteria. In particular, strains of Butyrivibrio fibrisolvens have been described that are cellulolytic (1, 21, 51), xylanolytic (12, 23), amylolytic (10), pectinolytic (68), lipolytic (20), and proteolytic (11,54). This ability to ferment a wide range of macromolecules is considered to enable B. fibrisolvens to be the most dominant rumen bacterium under adverse nutritional conditions. In winter, B. fibrisolvens is the most abundant starch-and cellulose-fermenting bacterium in the high-arctic Svalbard reindeer (43) and is unusual in its capacity to utilize both carbohydrate substrates whereas other cellulolytic species are unable to do so. B. fibrisolvens is also the most prevalent bacterium in the rumen of semistarved Zebu cattle in Kenya (35).Starch is an important component of the ruminal diet, and its digestion is essential for maximum productivity. Highstarch diets are, however, associated with a number of digestive disorders. For example, lactate acidosis is associated with a proliferation of the amylolytic species Streptococcus bovis and is thought to occur as a result of the rapid fermentation of starch leading to an accumulation of lactic acid (53). A knowledge of the nature and regulation of amylolytic enzymes could therefore assist in controlling these digestive disorders and improving the efficiency of starch digestion. Relatively few amylases of ruminal bacteria have been characterized. Those that have been studied include amylases from S. bovis, Clostridium butyricum (24, 65), and Ruminobacter amylophilis (formerly Bacteroides am...

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Section: Resultsmentioning

confidence: 99%

Cloning, nucleotide sequence, and enzymatic characterization of an alpha-amylase from the ruminal bacterium Butyrivibrio fibrisolvens H17c

et al. 1991

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“…These results indicate that this enzyme acts on polysaccharides exowisely by removing G 6 successively from their non-reducing ends. Exomaltohexaohydrolase (EC 3.2.1.98) of Aerobacter aerogenes 16 ) is a well-known G 6 -forming amylase. B. circulans F-2 amylase is the second example of a G 6 -forming amylase but differs from that of A. aerogenes in its high activity on G 6 .…”

Section: Discussionmentioning

confidence: 99%

Purification ofBacillus circulansF-2 Amylase and Its General Properties

Taniguchi

Chung

Yoshigi

et al. 1983

Agricultural and Biological Chemistry

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“…2IU/mg-protein . 3) Properties of the enzyme Figure 3 shows pH-activity and pH-stability of the enzyme.…”

Section: And Discussionmentioning

confidence: 99%

Purification and some properties of an extracellular exo-maltohexaohydrolase from an Aerobacter aerogenes mutant.

Nakakuki

Azuma

Monma

et al. 1982

Journal of the Japanese Society of Starch Science

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Purification and some properties of a novel maltohexaose-producing exo-amylase from Aerobacter aerogenes

Cited by 48 publications

References 21 publications

Cloning, nucleotide sequence, and enzymatic characterization of an alpha-amylase from the ruminal bacterium Butyrivibrio fibrisolvens H17c

Cloning, nucleotide sequence, and enzymatic characterization of an alpha-amylase from the ruminal bacterium Butyrivibrio fibrisolvens H17c

Purification ofBacillus circulansF-2 Amylase and Its General Properties

Purification and some properties of an extracellular exo-maltohexaohydrolase from an Aerobacter aerogenes mutant.

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