Partial Purification and Characterization of Acid and Neutral<i>α</i>-Glucosidases from Preclimacteric Banana Pulp Tissues

Konishi, Yôtarô; Kitazato, Sachiko; Nakatani, Nobuji

doi:10.1271/bbb.56.2046

Cited by 15 publications

(14 citation statements)

References 11 publications

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“…However, the relatively large increase in α-glucosidase activity with these substrates on complementation with the potato gene provides tentative evidence that this enzyme has a broad substrate specificity and acts at a low rate on amylopectin and boiled starch. This type of substrate specificity has previously been observed for α-glucosidases purified from banana pulp (Konishi et al, 1992), spinach (Sugimoto et al, 1997) and pea (Sun et al, 1995). Other α-glucosidases exhibit different substrate specificities, preferentially hydrolysing starch rather than malto-oligosaccharides (Konishi et al, 1992 and references therein) or not being active against soluble starch (Sun and Henson, 1990).…”

Section: Discussionsupporting

confidence: 76%

“…This type of substrate specificity has previously been observed for α-glucosidases purified from banana pulp (Konishi et al, 1992), spinach (Sugimoto et al, 1997) and pea (Sun et al, 1995). Other α-glucosidases exhibit different substrate specificities, preferentially hydrolysing starch rather than malto-oligosaccharides (Konishi et al, 1992 and references therein) or not being active against soluble starch (Sun and Henson, 1990). The pH optimum of the potato enzyme was 6.5 ( Figure 2a) and so the enzyme can be placed in the neutral α-glucosidase category (Konishi et al, 1992).…”

Section: Discussionsupporting

confidence: 76%

“…Other α-glucosidases exhibit different substrate specificities, preferentially hydrolysing starch rather than malto-oligosaccharides (Konishi et al, 1992 and references therein) or not being active against soluble starch (Sun and Henson, 1990). The pH optimum of the potato enzyme was 6.5 ( Figure 2a) and so the enzyme can be placed in the neutral α-glucosidase category (Konishi et al, 1992). The apparent K m of the α-glucosidase activity was high (17 mM for maltose) although α-glucosidases with K m values in this range have been purified from pea chloro-plasts (Beers et al, 1990) and from Brewer's yeast (Konishi et al, 1992).…”

Section: Discussionmentioning

confidence: 99%

“…Examples of acid α-glucosidases (pH optimum 4-5) include those isolated from banana pulp tissue (Konishi et al, 1992); from the seeds of barley (Sun and Henson, 1990); buckwheat (Kanaya et al, 1976); flint corn (Chiba and Shimomura, 1975); green gram (Yamasaki and Suzuki, 1979); peas (Beers et al, 1990); rice (Takahashi et al, 1971); sugar beet (Yamasaki and Konno, 1991); and Welsh onion (Suzuki and Uchida, 1984). Neutral isoforms of α-glucosidase (pH optimum 6-7) have been isolated from potato tubers (Killilea and Clancy, 1978), banana pulp tissue (Konishi et al, 1992) and also from pea chloroplasts (Sun et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

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cDNA cloning and characterisation of an α‐glucosidase gene from potato (Solanum tuberosum L.)

Taylor¹,

George²,

Ross³

et al. 1998

The Plant Journal

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SummaryUsing an Arabidopsis thaliana expressed sequence tag with sequence similarity to human lysosomal α-glucosidase as a probe, a potato cDNA was isolated. The cDNA encodes a polypeptide with an Mr value of 105,400 and the most significant matches of the deduced amino acid sequence are with members of family 31 of glucosyl transferase. The potato cDNA was expressed in a strain of Saccharomyces cerevisiae that is deficient in maltase activity and unable to grow using maltose as a carbon source (ABYSMAL81). Expression of the potato cDNA in the mutant yeast strain restores its ability to use maltose as a carbon source for growth. Additionally, α-glucosidase activity could be measured in extracts of the yeast cells following complementation. A range of maltodextrins were substrates for this activity. The steady-state expression level of the potato α-glucosidase gene was low in most tissues examined, the highest levels occurring in sprouting tubers and source leaves.

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Section: Discussionsupporting

confidence: 76%

Section: Discussionsupporting

confidence: 76%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

cDNA cloning and characterisation of an α‐glucosidase gene from potato (Solanum tuberosum L.)

Taylor¹,

George²,

Ross³

et al. 1998

The Plant Journal

View full text Add to dashboard Cite

show abstract

“…[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20], -II (Frs. 39-64), and -III (Frs.…”

Section: Resultsunclassified

Isolation and Characterization of aβ-Primeverosidase Concerned with Alcoholic Aroma Formation in Tea Leaves

Guo

Ogawa

Yamauchi

et al. 1996

Bioscience, Biotechnology, and Biochemistry

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Probing the catalytic site of rabbit muscle glycogen phosphorylase using a series of specifically modified maltohexaose derivatives

et al. 2017

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Glycogen phosphorylase (GP) is an allosteric enzyme whose catalytic site comprises six subsites (SG, SG, SG, SG, SG, and SP) that are complementary to tandem five glucose residues and one inorganic phosphate molecule, respectively. In the catalysis of GP, the nonreducing-end glucose (Glc) of the maltooligosaccharide substrate binds to SG and is then phosphorolyzed to yield glucose 1-phosphate. In this study, we probed the catalytic site of rabbit muscle GP using pyridylaminated-maltohexaose (Glcα1-4Glcα1-4Glcα1-4Glcα1-4Glcα1-4GlcPA, where GlcPA = 1-deoxy-1-[(2-pyridyl)amino]-D-glucitol]; abbreviated as PA-0) and a series of specifically modified PA-0 derivatives (Glc -AltNAc-Glc -GlcPA, where m + n = 4 and AltNAc is 3-acetoamido-3-deoxy-D-altrose). PA-0 served as an efficient substrate for GP, whereas the other PA-0 derivatives were not as good as the PA-0, indicating that substrate recognition by all the SG -SG subsites was important for the catalysis of GP. By comparing the initial reaction rate toward the PA-0 derivatives (V ) with that toward PA-0 (V), we found that the value of V /V decreased significantly as the level of allosteric activation of GP increased. These results suggest that some conformational changes have taken place in the maltooligosaccharide-binding region of the GP catalytic site during allosteric regulation.

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Partial Purification and Characterization of Acid and Neutralα-Glucosidases from Preclimacteric Banana Pulp Tissues

Cited by 15 publications

References 11 publications

cDNA cloning and characterisation of an α‐glucosidase gene from potato (Solanum tuberosum L.)

cDNA cloning and characterisation of an α‐glucosidase gene from potato (Solanum tuberosum L.)

Isolation and Characterization of aβ-Primeverosidase Concerned with Alcoholic Aroma Formation in Tea Leaves

Probing the catalytic site of rabbit muscle glycogen phosphorylase using a series of specifically modified maltohexaose derivatives

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