Multiple forms of α-glucan phosphorylase in banana fruits: Properties and kinetics

Singh, Surjeet; Sanwal, G.G.

doi:10.1016/s0031-9422(00)88914-1

Cited by 20 publications

(16 citation statements)

References 25 publications

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“…A previous report by Yang and Ho (1958) on the increase of phosphorylase activity during the climacteric rise of respiration is contrary to what was observed in this laboratory. However, those researchers did not properly protect the enzyme from inactivation by phenolics during the extraction procedures which may also explain the low initial (70% less) phosphorylase activity they detected.…”

Section: Discussioncontrasting

confidence: 99%

“…The results about the development of soluble sugars during ripening of bananas that have previously been reported in the literature have not been conclusive. In some cases the content of glucose plus fructose predominates over that of sucrose (Barnell 1940;Biale 1960;Eheart and Mason 1967), while others have observed the opposite for the same period of ripening (Gane 1971;Poland et al 1938;Yang and Ho 1958).…”

Section: Discussionmentioning

confidence: 99%

“…the observation that the activity of phosphatase increased during the climacteric phase Yang and Ho (1958) suggested that this enzyme might be more important to the ripening process than the amylases. A similar conclusion was reached by Surendranathan and Nair (1973) for earlier stages of ripening.…”

mentioning

confidence: 99%

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Starch Transformation During Banana Ripening: I ? The Phosphorylase and Phosphatase Behavior in Musa Acuminata

Arêas

Lajolo

1981

J Food Biochemistry

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Starch levels as well as the phosphorylases and acid phosphatase activity during ripening of the banana fruit was investigated. The concentrations and sequence of appearance of sucrose, glucose and fructose were determined by use of specific enzymatic reactions. During the climacteric period, the phosphatase activity increased while phosphorylase activity, which initially increased before starch transformation began, thereafter decreased in a complex pattern. The starch was transformed into sucrose with later formation of glucose and fructose. Four bands of phosphorylase multiple forms, detected electrophoretically, did not change during ripening. One of them was able to synthesize a branched starch‐using amylose as a primer and glucose 1 ‐phosphate as the substrate. Banana slices were infiltrated with water or solutions of cycloheximide or actinomycin D. Inhibition of phosphatase‐induced activity was recorded only in the cycloheximide group. No change in phosphorylase activity was detected in any of these infiltrated groups. Sucrose production from starch was partially inhibited both by actinomycin D and cycloheximide. The aformentioned results were interpreted as indicating the previous presence of phosphorylase in the preclimacteric phase without new synthesis during ripening. The increase of activity of phosphatase was probably due to ribosomal synthesis rather than to nucleic acid synthesis.

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Section: Discussioncontrasting

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Starch Transformation During Banana Ripening: I ? The Phosphorylase and Phosphatase Behavior in Musa Acuminata

Arêas

Lajolo

1981

J Food Biochemistry

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“…A large difference in the Km values of starch phosphorylases for the primer has been reported. Singh & Sanwal (1976) reported the Km values for starch as 0.24,0.95, and 1.21 g/L, respectively, for three different forms of banana fruit phosphorylase. Preiss et al (1980) reported the Km values for amylose as 0.165 and 0.122 g/L for cytoplasmic and chloroplastic phosphorylase, respectively.…”

Section: Discussionmentioning

confidence: 99%

Purification and physicochemical properties of starch phosphorylase from young banana leaves

Kumar¹,

Sanwal²

1982

Biochemistry

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Starch phosphorylase from young banana leaves has been purified to homogeneity, as tested by disc polyacrylamide gel electrophoresis at various pHs and gel concentrations, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, immunodiffusion, and immunoelectrophoresis, using the techniques of ammonium sulfate fractionation, DEAE-cellulose chromatography, and filtration through Sephadex G-100 and Sephadex G-200. The molecular weight of the enzyme is found to be 45000 as determined by gel filtration chromatography over Sephadex G-200. The enzyme showed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis having the molecular weight 55000. The enzyme contains eight SH groups per mol of the enzyme. Unlike other 1,4-alpha-glucan phosphorylases, no evidence is found for the presence of pyridoxal 5'-phosphate as a prosthetic group of the enzyme. Of the various amino acids tested, only aromatic amino acids inhibited the enzyme activity. ADP, AMP, and 3',5'-AMP did not produce any effect on the enzyme activity whereas ATP and UDP-glucose proved to be inhibitors. The enzyme utilized starch, amylose, and glycogen as primers with equal efficiency whereas dextrin, amylopectin, maltotriose, and maltose were less effective as primers. Schardinger dextrin, cellulose, or sucrose could not be utilized as a primer. The enzyme showed absolute specificity for glucose 1-phosphate as a substrate, and this could not be replaced by glucose-6-phosphate, fructose-6-phosphate, fructose 1,6-bisphosphate, or ribose 5-phosphate.

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“…A similar observation was made by Surendranatham and Nair (18) but for earlier stages of ripening. Singh and Sanwall (15,16,17) partially purified three phosphorylase forms from ripe bananas and observed different biochemical characteristics but did not investigate the behavior of these enzymes during ripening.…”

Section: They Also Detected the Presence Of P-amylase And Phosphorylasementioning

confidence: 99%

Phosphorylase, Phosphatase, α-Amylase Activity and Starch Breakdown during Ripening of ‘Marmelo’ Banana [(Musa acuminata Colla) × (Musa balbisiana Colla) ABB Group] Whole Fruit and Thin Slices1

Chitarra

Lajolo²

1981

J. Amer. Soc. Hort. Sci.

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Starch hydrolysis, phosphorylase, phosphatase and α-amylase activity of ‘Marinelo’ banana (Musa acuminata Colla × Musa balbisiana Colla, ABB group) during ripening of whole fruit and thin slices infiltrated with water (controls), cycloheximide and actinomycin D were investigated. Phosphatase and α-amylase activity of whole fruit increased during the climacteric while phosphorylase decreased as starch degradation proceded. Starch degradation had a different temperature coefficient than that of α-amylase activity when the storage temperature was raised from 20 to 25°C and stopped when 25% of the starch was still present. Activity of α-amylase in slices infiltrated with water, increased before the onset of the climacteric as a result of injury and at the same time starch was being hydrolyzed. Cycloheximide inhibited this induced activity increase but not starch breakdown or the increase of activity which occurs during the climacteric. Actinomycin D did not inhibit the α-amylase increase and its effect was a general retardation of ripening.

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Multiple forms of α-glucan phosphorylase in banana fruits: Properties and kinetics

Cited by 20 publications

References 25 publications

Starch Transformation During Banana Ripening: I ? The Phosphorylase and Phosphatase Behavior in Musa Acuminata

Starch Transformation During Banana Ripening: I ? The Phosphorylase and Phosphatase Behavior in Musa Acuminata

Purification and physicochemical properties of starch phosphorylase from young banana leaves

Phosphorylase, Phosphatase, α-Amylase Activity and Starch Breakdown during Ripening of ‘Marmelo’ Banana [(Musa acuminata Colla) × (Musa balbisiana Colla) ABB Group] Whole Fruit and Thin Slices1

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