• P Manjunath

      Articles written in Journal of Biosciences

    • Comparative studies on glucoamylases from three fungal sources

      P Manjunath M R Raghavendra Rao

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      Five commercial preparations of glucoamylases (three fromAspergillus niger, one each fromAspergillus foetidus andAspergillus candidus) were purified by ultrafiltration, Sepharose-gel filtration and DEAE-sephadex chromatography. Two forms of the enzyme, namely glucoamylase I and glucoamylase II were obtained from the fungi except from one strain ofA. Niger. All the enzymes appeared homogeneous by electrophoresis and ultracentrifugation. The specific activities varied between 85 and 142 units. The pH and temperature optima were between 4 and 5, and 60‡C respectively. The molecular weight as determined by the sodium dodecyl sulphate-polyacrylamide gel electrophoresis ranged from 75,000 to 79,000 for glucoamylase I and 60,000 to 72,000 for glucoamylase II. OnlyA. niger glucoamylases contained phenylalanine at the N-terminal end. The amino acid composition of the enzymes was generally similar. However,A. niger andA. foetidus glucoamylases, in contrast toA. candidus enzymes, contained greater percentage of acidic than of basic amino acids. The enzymes contained 15 to 30% carbohydrate and 49 to 57 residues of monosaccharides per mol.A. niger enzymes contained mannose, glucose, galactose, xylose and glucosamine but theA. candidus enzyme lacked xylose and glucose and only xylose was absent inA, foetidus enzymes. Majority of the carbohydrate moieties were O-glycosidically linked through mannose to the hydroxyl groups of seline and threonine of the polypeptide chain.

    • Immunochemical relationship between glucoamylases I and II ofAspergillus niger

      P Manjunath M R Raghavendra Rao

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      Rabbit antisera were prepared against the purified glucoamylases I and II ofAspergillus niger. Relationships between the two enzyme forms were investigated by using the antisera in immunodiffusion and immunoinhibition experiments. Both the forms of glucoamylase gave a single continuous precipitin band demonstrating very close structural resemblance. They gave almost identical immunoprecipitation patterns and had the same equivalence points indicating that the two forms ofA. niger gluoamylases were immunologically identical. The enzyme treated with periodate was immunologically identical with the controls and had slightly less enzyme activity but showed greatly reduced stability on storage at 4‡ C.

    • Studies on carbohydrate moieties ofAspergillus niger glucoamylase II: Isolation, purification and characterization of glycopeptides

      P Manjunath M R Raghavendra Rao

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      Six glycopeptide fractions namely GP-C1, GP-C2. GP-C3a.GP-C3b.GP-D, and GP-D2 were isolated after exhaustive digestion of glucoamylase II (Glucozyme) fromAspergillus niger with pronase. They were purified using gel-filtration. high-voltage paper electrophoresis and ion-exchange chromatography on Dowex-50 and Dowex-1. They appeared homogeneous on electrophoresis under different conditions of pHs. The molecular weights ranged from 1600 and 4000 for these glycopeptides. Ally of them contained serine at the N-terminal end. Serine and threonine were the major amino acids with glycine, alanine, proline and tryosine present as minor constituents. Carbohydrate analysis revealed the presence of different sugars. Based on this, the glycopeptides were grouped into three types: (1) GP-C1 and GP-C2 containing mannose, glucose and galactose; (2) GP-C3a, and GP-C3b,containing mannose glucose and glucosamine; and (3) GP-D1 and GP-D2, containing mannose. glucose, galactose and xylose. Most sugar constituents in each glycopeptide occured in non-integral ratios implying a microheterogeneity of the carbohydrate moiety inAspergillus niger glucoamylase.

    • Studies on carbohydrate moieties of the glycoprotein, glucoamylase II ofAspergillus niger: Nature of carbohydrate-peptide linkage and structure of oligosaccharides

      P Manjunath M R Raghavendra Rao

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      Electrophoretically homogeneous type 1 (GP-C1 and GP-C2), type 2 (GP-C3a and GP-C3b,) and type 3 (GP-D1, and GP-D2) glycopeptides fromAspergillus niger glucoamylase II (Manjunath and Raghavendra Rao, preceding paper) were separately treated with alkaline borohydride. The (\-eliminated oligosaccharides were subjected to single and sequential digestion with specific glycosidases and the products analysed by gas liquid chromatography. The studies revealed that carbohydrate moieties were present as mannose, Man-Man-, and trisaccharide structures, namely, (a) GIc-Man-Man-, (b) Gal-Man-Man, (c) Man-Man-Man-, (d) GlcNAc-Man-Man-, and (e) Xyl-Man-Man. None of the glycopeptides contained all the trisaccharide structures (a) to (e). Type 1 glycopeptide contained structures (a), (b) and (c); type 2, (a) and (d) and type 3, (a), (b) and (e). The number of carbohydrate units (mono-, di-and trisaccharides) present in the major glycopeptides was determined and tentative structures for the glycopeptides proposed. Carbohydrate units appeared to occur in clusters of 4 to 7 in each glycopeptide, a structure unique to the carbohydrate moiety inAspergillus niger glucoamylase. Based on carbohydrate analysis and yields of glycopeptide, the number of units of each type of glycopeptide present in glucoamylase II was tentatively calculated to give two of type Man:Glc:Gal = 12–15:l:l, one of type Man:Glc:GlcN = 10-l1:1:2 and one of type Man :GIc :Gal:Xyl = 4–8:0.1:0.5-0.8:0.3-1 glycopeptides.

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      Plant mitochondria are quite distinct and have unique features, such as a cyanide-insensitive alternate pathway. They also interact with chloroplasts to optimize photosynthetic carbon assimilation.

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