Abstract
The oligosaccharidases and the transglycosylases occupy a key position in the biological activities of plants because by their action they provide the cells with the simple sugars entering the various pathways involved in the production of energy. They receive their specific substrates either from the breakdown of reserve and structural polysaccharides or directly from the chain of reactions summarized as photosynthesis.
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Literature
Adams, M., N. K. Richtmyer and C. S. Hudson: Some Enzymes present in highly purified Invertase Preparations; a contribution to the study of fructofuranosidases, galactosidases, glucosidases and mannosidases. J. Amer. Chem. Soc. 65, 1369 (1943).
Albon, N., D. J. Bell, P. H. Blanchard, D. Gross and J. T. Rundell: Kestose: a trisaccharide formed from sucrose by yeast invertase. J. Chem. Soc. (Lond.) 1953, 24.
Anagnostopoulos, C., J. E. Courtois and F. Petek: Transferring action of the α-galactosidase of coffee beans. Bull. Soc. Chim. biol. Paris 36, 1115 (1954).
Antoniani, C.: Osservazioni sulla β-glucosidasi del Sorghum saccharatum. Real. Ist. lombardo Sci. e Lett., Rend. (2) 68, 355–362 (1935).
Aristovskaya, T. V.: Enzyme activity of northern strains of microorganisms. Mikrobiologiya 17, 350 (1948).
Aronson, M.: Transgalactosidation during lactose hydrolysis. Arch. of Biochem a. Biophysics 39, 370 (1952).
Baba, T.: Über die besonderen Verhältnisse bei der Phosphorylierung von Maltose durch frische untergärige Hefe, Trockenhefe und Mazerationssaft. Biochem. Z. 273, 207 (1934).
Bacon, J. S. D.: Transfructosidation by a Yeast Invertase Preparation. Biochemie. J. 50, XVIII (1952).
The oligosaccharides produced by the action of yeast invertase preparations on sucrose. Biochemie. J. 57, 320 (1954).
Bacon, J. S. D., and D. J. Bell: A new trisaccharide produced from sucrose by mold invertase. J. Chem. Soc. (Lond.) 1953, 2528.
Bacon, J. S. D., and J. Edelman: The action of invertase preparations. Arch. of Biochem. 28, 467 (1950).
Bamann, E., u. K. Myrbäck: Die Methoden der Fermentforschung, Bd. 2. Leipzig: Georg Thieme 1941.
Baranovskii, P.M.: Biochemical processes in sprouting of soybean seeds. Izv. Akad. Nauk. Kazakh. SSSR., Ser. Fiziol. i. Biokhim. Rastenii 1947, No 2, 44.
Barker, S. A., and E. J. Bourne: Oligosaccharides synthesized from maltose by Escherichia coli. J. Chem. Soc. (Lond.) 1952, 209.
Barker, S. A., E. J. Bourne and T. R. Carrington: Aspergillus niger. III. Structure of a trisaccharide synthesized from sucrose. J. Chem. Soc. (Lond.) 1954, 2125.
Barker, S. A., E. J. Bourne, G. C. Hewitt and M. Stacey: Aspergillus niger. IV. Synthesis of β-linked glucosaccharides. J. Chem. Soc. (Lond.) 1955, 3734.
Barker, S. A., E. J. Bourne and M. Stacey: Aspergillus niger. I. The structure of the polyglucosan synthesized by Aspergillus niger 152. J. Chem. Soc. (Lond.) 1953, 3084.
Barker, S. A., and T. R. Carrington: Aspergillus niger. II. Transglycosidation by Aspergillus niger. J. Chem. Soc. (Lond.) 1953, 3588.
Bau, A.: Über ein neues Enzym der Hefe. Chemiker-Ztg 19, 1873–1874 (1895).
Bauer, C. R., and C. L. Gemmill: The heat produced by the enzymic action of the sucrose-invertase and urea-urease systems. Arch. of Biochem. a. Biophysics 35, 110 (1952).
Bealing, F. J.: Mould Glucosaccharase”: a Fructosidase. Biochemie. J. 55, 93 (1953).
Bell, D. J., and J. Edelman: Disaccharide synthesis following fructose transfer from sucrose by yeast invertase. J. Chem. Soc. (Lond.) 1954, 4652.
Berthelot, M.: Über die Produkte der Gärung des Zuckers. C. r. Acad. Sci. Paris 50, 980–984 (1860).
Blanchard, P. H., and N. Albon: The inversion of sucrose; a complication. Arch. of Biochem. 29, 220 (1950).
Bourquelot, E.: C. r. Acad. Sci. Paris 97, 1322 (1883); 116, 826 (1893).
Bourquelot, E., et A. Aubry: Influence de l’acide acétique sur les propriétés synthétisantes et hydrolysantes de la glucosidase α. J. Pharm. et Chim. (7) 12, 15 (1915).
Influence de la soude sur les propriétés synthétisantes et la glucosidase α. J. Pharm. et Chim. (7) 12, 182 (1915).
Synthèse biochim. d’un galactobiose. J. Pharm. et. Chim. (7) 14, 65 (1917).
Krystallisation und Eigenschaften der früher durch biochemische Synthese erhaltenen Galaktobiose. J. Pharm. et Chim. (7) 15, 246–249 (1917).
Synthèse biochim. d’un deuxième galactobiose. J. Pharm. et Chim. (7) 15, 273 (1917).
Bourquelot, E., et M. Bridel: Synthèse biochim. des glucosides d’alcools polyvalents; glucosides α de la glycérine et du glycol. J. Pharm. et Chim. (7) 8, 489, 547 (1913a).
Bourquelot, E., et H. Hérissey: Synthèse biochim. d’un glucoside isomère de la salicine, le salicylglucoside β. J. Pharm. et Chim. (7) 8, 49 (1913b).
Bourquelot, E., H. Hérissey et M. Bridel: Synthesen von α-Glucosiden mit Hilfe von α-Glucosidase, einem in der an der Luft getrockneten, untergärigen Hefe enthaltenen Enzym: α-Methyl- und α-Äthylglucosid. J. Pharm. et Chim. (7) 7, 145–154 (1913c).
Synthèse biochim. des glucosides d’alcools (glucosides α). III. Propylglucoside α et allylglucoside α. J. Pharm. et Chim. (7), 7, 525 (1913c).
Bourquelot, E., H. Hérissey et J. Coirre: Synthèse biochimique d’un sucre du groupe des hexobioses, le gentiobiose. C. r. Acad. Sci. Paris 157, 732 (1913d).
Brown, H. T., u. J. Heron: Über die hydrolytische Wirkung des Pankreas und des Dünndarms. Liebigs Ann. 204, 228 (1880).
Buchanan, J. G., J. A. Bassham, A. A. Benson, D. F. Broadlay, M. Calvin, L. L. Daus, M. Goodman, P.M.Hayes, V. H. Lynch, L. T. Norris and A.T.Wilson: The rôle of phosphate in the metabolism of photosynthetic organisms. In: A Symposium on Phosphorus Metabolism, vol. II, p. 440. Edited by W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Press 1952.
Bunton, C. A., T. A. Lewis, D. R. Llewellyn, H. Tristram and C. A. Vernon: Hydrolysis of methylglucosides. Nature (Lond.) 174, 560 (1954).
Buston, H. W., and A. Jabbar: Synthesis of β-linked glucosaccharides by extracts of Chaetomium globosum. Biochim. et Biophysica Acta 15, 543 (1954).
Caputto, R., L. F. Leloir, C. E. Cardini and A. C. Paladine: Isolation of the coenzyme of the galactose phosphate-glucose phosphate transformation. J. of Biol. Chem. 184, 333 (1950).
Caputto, R., L. F. Leloir u. R. E. Trucco: Lactase and lactose fermentation in Saccharomyces fragilis. Enzymologia (Den Haag) 12, 350 (1948).
Cohn, M.: Mechanisms of cleavage of glucose-1-phosphate. J. of Biol. Chem. 180, 771 (1949).
Cohn, M., and J. Monod: Purification and properties of the β-galactosidase (lactase) of Escherichia coli. Biochim. et Biophysica Acta 7, 153 (1951).
Cohn, M., and A. M. Torriani: Relationships in biosynthesis of the β-galactosidase and Pz proteins in Escherichia coli. Biochim. et Biophysica Acta 10, 280 (1953).
Courtois, J. E., C. Anagnostopoulos and F. Petek: Action of α-galactosidase on stachyose. Isolation of saccharose and raffinose. Enzymologia (Den Haag) 17, 69 (1954).
Crook, E. M., and B. A. Stone: Formation of oligosaccharides during the enzymic hydrolysis of β-glucosides. Biochemic. J. 55, XXV (1953).
Dam, B. van, J. G. Revallier-Warffemius and L. C. van Dam-Schermerhorn: Preparation of lactase from Saccharomyces fragilis. Netherlands Milk Dairy J. 4, 96 (1950).
Davies, R.: Enzyme formation in Saccharomyces fragilis. I. Invertase and Raffinase. Biochemic. J. 55, 484 (1953).
Dieu, H. A.: Invertase Studies. I. Bull. Soc. chim. Belg. 55, 306 (1947).
Invertase Studies. II. Bull. Soc. chim. Belg. 55, 327 (1947).
Edelman, J.: Transfer reactions catalysed by some sucrase preparations. Biochemie. J. 57, 22 (1954).
Elander, M., and K. Myrbäck: Isolation of crystalline trehalose after fermentation of glucose by maceration juice. Arch. of Biochem. 21, 249 (1949).
Fischer, E.: Einfluß der Configuration auf die Wirkung der Enzyme. I. Ber. dtsch. chem. Ges. 27, 2985–2993 (1894).
Einfluß der Configuration auf die Wirkung der Enzyme. II. Ber. dtsch. chem. Ges. 27, 3479–3483 (1894).
Über den Einfluß der Configuration auf die Wirkung der Enzyme. III. Ber. dtsch. chem. Ges. 28, 1429–1438 (1895).
Fischer, E., u. E. F. Armstrong: Synthese einiger neuer Disaccharide. Ber. dtsch. chem. Ges. 35, 3144–3153 (1902).
Fischer, E. H., u. L. Kohtès: Purification de l’invertase de levure. Helvet. chim. Acta 34, 1123 (1951).
Fischer, E. H., L. Kohtès u. J. Fellig: Propriétés de l’invertase purifiée. Helvet. chim. Acta 34, 1132 (1951).
Fitting, C., and M. Doudoroff: Phosphorolysis of maltose by enzyme preparations from Neisseria meningitidis. J. of Biol. Chem. 199, 153 (1952).
French, D.: Structure of Pan’s crystalline trisaccharide. Science (Lancaster, Pa.) 113, 352 (1951).
The raffinose family of oligosaccharides. Adv. Carbohydrate Chem. 9, 149 (1954).
French, D., G. M. Wild and W. J. James: Constitution of stachyose. J. Amer. Chem. Soc. 75, 3664 (1953).
Fujii, M.: Studies on sugarcane invertase. I. Leaf invertase. J. Agric. Chem. Soc. Jap. 18, 961 (1942).
Studies on sugar-cane invertase. II. Distribution of invertase in the leaves and its enzymic chemical properties. J. Agric. Chem. Soc. Jap. 20, 421 (1944).
Gillespie, J. M., M. A. Jermyn and E. F. Woods: Multiple nature of the enzymes of Aspergillus oryzae and of horse-radish. Enzymes of Aspergillus oryzae. Nature (Lond.) 169, 487 (1952).
Gilliland, R. B.: A yeast hybrid heterozygotic in four fermentation characters. C. r. Labor. Carlsberg, Ser. Physiol. 24, 347 (1949).
Gottschalk, A.: The proportion of fructo-furanose present in d-fructose solution at equilibrium (0°C). Austral. J.Exper. Biol. a.Med. Sci. 21, 139 (1943).
The effect of temperature on the fermentation of d-mannose by yeast. Biochem. J. 41, 276 (1947).
Mechanism of enzyme specificity in the domain of carbohydrates. Nature (Lond.) 160, 113 (1947).
“Direct” fermentation of disaccharides by yeast. A critical discussion. Wallerstein Lab. Communications 12, 55 (1949).
Principles underlying enzyme specificity in the domain of carbohydrates. Adv. Carbohydrate Chem. 5, 49 (1950).
α-d-Glucosidases. In: The Enzymes. Chemistry and Mechanism of Action. Vol. I, part. 1, p. 551. Edited by J. B. Sumner and K. Myrbäck. New York: Academic Press 1950.
On the Mechanism of Enzyme Action. Rev. Pure a. Appl. Chem. 3, 179 (1953).
Gross, D.: Paper electrophoresis of the oligosaccharides synthesized from sucrose by yeast invertase. Nature (Lond.) 173, 487 (1954).
Gross, D., P.H.Blanchard and D. J. Bell: Neo-kestose; a trisaccharide formed from sucrose by yeast invertase. J. Chem. Soc. (Lond.) 1954, 1727.
Halvorson, H. O., and S. Spiegelman: The inhibition of enzyme formation by amino acid analogues. J. Bacter. 64, 207 (1952).
Hassid, W. Z.: Biosynthesis of complex saccharides. Contribution to ‘Chemical Pathways of Metabolism’, Vol. I, p. 235–275. Edited by D. M. Greenberg. New York: Academic Press 1954.
Hassid, W. Z., and M. Doudoroff: Synthesis of disaccharides with bacterial enzymes. Adv. Enzymol. 10, 123 (1950).
Hassid, W. Z., M. Doudoroff, A. L. Potter and H. A. Barker: Structure of an enzymatically synthesized reducing disaccharide, d-glucosido-L-arabinose. J. Amer. Chem. Soc. 70, 306 (1948).
Hattori, S., and T. Siroya: Sugars in the seeds and seedlings of Pinus thunbergi. Bot. Mag. (Tokyo) 64, 137 (1951).
Hehre, E. J.: The biological synthesis of dextran from dextrins. J. of Biol. Chem. 192, 161 (1951).
Hehre, E. J., and A. S. Carlson: Evidence on the constitution of melezitose through degradation to sucrose by bacterial action. Arch. of Biochem. a. Biophysics 36, 158 (1952).
Helferich, B.: Emulsin. Erg. Enzymforsch. 7, 83–104 (1938).
Enzyme Specificity. In: The Enzymes. Chemistry and Mechnisms of Action. Vol. 1, part. 1, p. 79. Edited by J. B. Sumner and K. Myrbäck. New York: Academic Press 1950.
Helferich, B., S. Demant, J. Goerdeler u. R. Bosse: Über die Carbohydrasen des Gerstenmalzes, das „Malz-Emulsin“. Hoppe-Seylers Z. 283, 179–186 (1948).
Helferich, B., u. H. Rauch: Zucker-Synthesen, IV. 6-β-d-Galaktosido-d-glucose, ein Beitrag zur Konstitution der Melibiose. Ber. dtsch. chem. Ges. 59, 2655 bis 2657 (1926).
Helferich, B., u. G. Sparmberg: Krystallisierte 6-β-d-Galaktosido-d-glucose. Ber. dtsch. chem. Ges. 66, 806–807 (1933).
Helferich, B., u. F. V. Stryk: Methansulfonsäureester in der Zuckergruppe. V. Mitt. Über die Ferment-Spaltung von Trehalose. Ber. dtsch. chem. Ges. 74, 1794–1798 (1941).
Helferich, B., u. F.Vorsatz: Über Kaffee-Emulsin. Emulsin XXV. Hoppe-Seylers Z. 237, 254–260 (1935).
Hérissey, H.: Sur l’hydrolyse du méthyle-d-mannoside-α par des ferments solubles. C. r. Acad. Sci. Paris 172, 766–768 (1921).
Hestrin, S.: Specificity of mold maltase. Enzymologia (Den Haag) 8, 193 (1940).
Hestrin, S., and C. C. Lindegren: Carbohydrases in Saccharomyces Haploid Stocks of Defined Genotype. II. Gene-Controlled Induction of Glucosidases by α-Glucosides. Arch. of Biochem. a. Biophysics 38, 317 (1952).
Hill, K.: Über Luzerneemulsin. Ber. Verh. sächs. Akad. Wiss. Leipzig, Math.-phys. Kl. 86, 115–128 (1934).
Hoeckner, E.: Die Rohrzuckerspaltung durch Bacterium coli. Z.Hyg. 129, 519–537 (1949).
Hofmann, E.: Untersuchungen über Glykoside- und Disaccharide-spaltende Enzyme von Schimmelpilzen. Biochem. Z. 272, 133 (1934a).
Vorkommen von Maltase und Saccharase bei Schizosaccharomyces octosporus (Beijerinck) und deren Trennung. Biochem. Z. 272, 417 (1934b).
Neues zur Frage nach der Spezifität der Glykosidasen, insbesondere bei Schimmelpilzen und Bakterien. Naturwiss. 22, 406–409 (1934c).
Hofmann, E., u. E. Latzko: Einflüsse der Nährstoffe Kali und Stickstoff auf Fermentgehalt und Qualität pflanzlicher Erzeugnisse. Biochem. Z. 321, 476–481 (1951).
Hofmann, E., u. H. Scheck: Über die Trennung von β-Glukosidase und β-Galactosidase bei Milchzuckerhefen. Biochem. Z. 319, 522–528 (1949).
Hogness, D. S., M. Cohn and J. Monod: Studies on the induced synthesis of β-galactosidase in Escherichia coli: The kinetics and mechanism of sulphur incorporation. Biochim. et Biophysica Acta 16, 99 (1955).
Isaiev, V. J.: The maltase of yeast. J. Inst. Brewing 32, 552 (1926).
Ishii, R., and S. Akagi: Studies on Monilia sitophila. II. Enzymes produced. Hakkô Kôgaku Zasshi (J. Fermentation Technol.) 26, 276 (1948).
Jermyn, M. A.: Fungal Cellulases. VI. Substrate and inhibitor specificity of the β-glucosidase of Stachybotrys atra. Austral. J. Biol. Sci. 8, 577 (1955).
Jermyn, M. A., and R. Thomas: Transferase activity of the β-glucosidase of Aspergillus oryzae. Austral. J. Biol. Sci. 6, 70 (1953).
Kalckar, H. M.: The mechanism of transglycosidation. In: A Symposium on the Mechanism of Enzyme Action, p. 675. Edited by W. D. Mc Elroy and B. Glass. Baltimore: Johns Hopkins Press 1954.
Kasparova, S.A., and A. M. Khristoforrova: Biochemical processes in ascertaining the winter hardiness of clover for arctic planting. Biokhimiya 13, 441 (1948).
Kharebava, G. I.: Enzymic processes in a living tea leaf. Biokhimiya Chaĭnago Proízvodstva Sbornik 1946, Nr 5, 86.
Kitahara, K., and M. Kurushima: The diastatic enzyme systems of moulds. I. Comparison of diastatic enzyme systems of several important moulds. Hakkô Kôgaku Zasshi (J. Fermentation Technol.) 27, 1 (1949).
Kobayashi, K.: Sugar-hydrolysing enzymes. VI. Differences between β-glucosidase and β-galactosidase. J. Jap. Biochem. Soc. 18, 41 (1944).
Koppel, J. L., C. J. Porter and B. F. Crocker: Mechanism of the synthesis of enzymes. I. Development of a system suitable for studying this phenomenon. J. Gen. Physiol. 36, 703 (1953).
Koshland, D.E.: Stereochemistry and the Mechanism of Enzymatic Reactions. Biol. Rev. 28, 416 (1953).
Koshland, D. E., and S. S. Stein: Enzyme specificity and enzyme mechanism. Federat.Proc. 12, 233 (1953).
Kuby, S. A., and H. A. Lardy: Purification and kinetics of β-d-galactosidase from Escherichia coli strain K-12. J. Amer. Chem. Soc. 75, 890 (1953).
Kuhn, R.: Saccharase- und Raffinasewirkung des Invertins. Hoppe-Seylers Z. 125, 28–92 (1923).
Lederberg, J.: The β-d-galactosidase of Escherichia coli strain K-12. J. Bacter. 60, 381 (1950).
Leloir, L. F., and E. Cabib: The enzymic synthesis of trehalose phosphate. J. Amer. Chem. Soc. 75, 5445 (1953).
Lester, G.: The β-galactosidase of lactose mutants of Escherichia coli K-12. Arch. of Biochem. a. Biophysics 40, 390 (1952).
Lindegren, C. C.: The Yeast Cell, its Genetics and Cytology. St. Louis: Educational Publishers 1949.
Lisitsyn, D.I.: Activity of carbohydrase in leaves of “glucoside” plants. Biokhimiya 18, 188 (1953).
Lukes, T. M., and H. J. Phaff: Characteristics of trehalase in Candida tropicalis. Antonie van Leeuwenhoek J. Microbiol. a. Serol. 18, 323 (1952).
Mandels, G. R.: Invertase of Myrothecium verrucaria spores. Amer. J. Bot. 38, 213 (1951).
Mehrotra, B. S.: Physiological studies of Phytophthora. I. Enzyme action. J. Indian Bot. Soc. 28, 108 (1949).
Michaelis, L., u. H. Davidsohn: Die Wirkung der H-Ionen auf das Invertin. Biochem. Z. 35, 386 (1911).
Michaelis, L., u. M. L. Menten: Die Kinetik der Invertin Wirkung. Biochem. Z. 49, 333 (1913).
Miwa, T.: Enzymic transfer of sugars. Symposia Enzyme Chem. (Japan) 8, 57 (1953).
Miwa, T., C. Cheng, M. Fujisaki and A. Toishi: The specificity of glucosidases. I. Relations between glucosidases of various origins and β-d-glucosides of various compositions. Acta Phytochim. (Tokyo) 10, 155 (1937).
Miwa, T., K. Takano, K. Mafune and S. Furutani: Glucotransferase. Proc. Japan. Acad. 25, 111 (1949).
Miwa, T., and K. Tanaka: Glycosidases of apricot emulsin. Symposia Enzyme Chem. (Japan) 2, 19 (1949).
Monod, J., G. Cohen-Bazire and M. Cohn: The biosynthesis of β-galactosidase (lactase) by Escherichia coli. Biochim. et Biophysica Acta 7, 585 (1951).
Monod, J., A. M. Torriani and J. Gribetz: Lactase extract from a stock of mutable Escherichia coli. C. r. Acad. Sci. Paris 227, 315 (1948).
Morita, Y.: β-Xylosidase. J. Jap. Biochem. Soc. 24, 189 (1952).
Myrbäck, K.: α-Glukosidase und Disaccharidspaltung. Hoppe-Seylers Z. 205, 248 (1932).
Myrbäck, K., u. U. Björklund: Activity-pH-curves of the enzymatic saccharose and raffinose hydrolysis. Ark. Kemi (Stockh.) 4, 567 (1952).
Narayanamurti, D., u. G. M. Verma: Cellulase and invertase from Polystictus sanguineus. The mechanism of wood-protective agents. Holz als Roh- u. Werkstoff 11, 7 (1953).
Nath, K., and H. N. Rydon: The influence of structure on the hydrolysis of substituted phenyl β-d-glucosides by emulsin. Biochemie. J. 57, 1 (1954).
Nelson, J. M., E. T. Palmer and B. G. Wilkes: Similarity of the kinetics of invertase action in vivo and in vitro. J. Gen. Physiol. 15, 491 (1932).
Nelson, J. M., and B. G. Wilkes: Similarity of the kinetics of invertase action in vivo and in vitro. III. J. Gen. Physiol. 16, 571 (1933).
Neuberg, C.: Zur Kenntnis der Raffinose. Abbau der Raffinose zu Rohrzucker und d-Galaktose. Biochem. Z. 3, 519–534 (1907).
Neuberg, C., u. E. Hofmann: Über enzymatische Spaltungen der Malto- und Lactobionsäure. Biochem. Z. 252, 434–439 (1932).
Neuberg, C., u. S. Lachmann: Zur Kenntnis der Stachyose. Biochem. Z. 24, 171–177 (1910).
Neuberg, C., and I. Mandl: Invertase. In: The Enzymes. Chemistry and Mechanism of Action. Vol. 1, part. 1, p. 527. Edited by J. B. Sumner and K. Myrbäck. New York: Academic Press 1950.
Nilsson, R., u. F. Alm: On the rôle of adenylpyrophosphatase in alcoholic fermentation and on the occurrence of trehalose during fermentation with maceration juice. Acta chem. scand. (Helsinki) 3, 213 (1949).
Nishizawa, K., and K. Wakabayashi: Enzymic breakdown of β-cellobioside. I. Specificity of the β-cellobioside-splitting enzymes of apricot and malt. J. Jap. Biochem. Soc. 24, 36 (1952).
Niwa, K.: Purification of β-glucosidase of Aspergillus niger II. J. of Biochem. (Tokyo) 38, 109 (1951).
Oppenheimer, C.: Die Fermente und ihre Wirkungen, 5. Aufl., Bd. 1. Leipzig: Georg Thieme 1925.
Pan, S. C., L. W. Nicholson and P. Kolachov: Isolation of a crystalline trisaccharide from the unfermentable carbohydrate produced enzymically from maltose. J. Amer. Chem. Soc. 73, 2547 (1951).
Enzymic synthesis of oligosaccharides: A transglycosidation. Arch. of Biochem. a. Biophysics 42, 406 (1953).
Pazur, J. H.: Transfructosidation reactions of an enzyme of Aspergillus oryzae. J. of Biol. Chem. 199, 217 (1952).
The mechanism of enzymatic synthesis of galactosyl oligosaccharides. J. of Biol. Chem. 208, 439 (1954).
Pazur, J. H., and D. French: The action of transglucosidase of Aspergillus oryzae on maltose. J. of Biol. Chem. 196, 265 (1952).
Peat, S., W. J. Whelan and K. A. Hinson: Synthetic action of almond emulsin. Nature (Lond.) 170, 1056 (1952).
Pigman, W. W.: Action of almond emulsin on the phenyl glycosides of synthetic sugars and on β-thiophenyl-d-glucoside J. Res. Nat. Bur. Stand. 26, 197–204 (1941).
Pigman, W. W.: Specificity, classification and mechanism of action of the glycosidases. Adv. Enzymol. 4, 41 (1944).
Pigman, W. W., and R. M. Goepp: Chemistry of the Carbohydrates. New York: Academic Press 1948.
Pringsheim, H., u. J. Leibowitz: Über Reversionssynthesen: I. Die Wirkung der Hefemaltase. Ber. dtsch. chem. Ges. 57, 1576 (1924).
Purves, C.B., and C. S. Hudson: Analysis of γ-methyl fructoside mixtures by means of invertase. I. J. Amer. Chem. Soc. 56, 702 (1934).
Analysis of γ-methyl fructoside mixtures by means of invertase. IV. Behaviour of sucrose in methanol containing hydrogen chloride. J. Amer. Chem. Soc. 56, 1973 (1934).
Putman, E. W., C. Fitting Litt and W. Z. Hassld: The structure of d-glucosyl-d-xylose synthesized by maltose phosphorylase. J. Amer. Chem. Soc. 77, 4351 (1955).
Rabaté, J.: Sur l’hydrolyse du salicoside par la poudre fermentaire de feuilles de Salix purpurea et sur quelques phénomènes qui en dérivent. Bull. Soc. chim. biol. Paris 17, 572 (1935).
Roberts, H. R., and E. F. Mc Farren: The Chromatographie observation of oligosaccharides formed during the lactase hydrolysis of lactose. J. Dairy Sci. 36, 620 (1953).
The formation of oligosaccharides during the lactase hydrolysis of lactose. Arch. of Biochem. a. Biophys. 43, 233 (1953).
Robinson, R., and W. T. J. Morgan: Trehalose monophosphoric ester isolated from the products of fermentation of sugars with dried yeast. Biochemie. J. 22, 1277 (1928).
Roy, D. K., and M. K. Roy: Amylases of butyl organisms. Science a. Culture (India) 18, 339 (1953).
Sadasivan, V.: The phosphatases in coconut (Cocos nucifera). Arch. of Biochem. 30, 159 (1951).
Saksena, R. K., and S. K. Bose: Enzymes of two water moulds. J. Indian Bot. Soc. 23, 108 (1944).
Saroja, K., R. Venkataraman and K. V. Gibi: Transglucosidation in Penicillium chrysogenum Q-176. Biochemie. J. 60, 399 (1955).
Sisakyan, N.M., and A.M. Kobyakova: Enzymic activity of protoplasmic structures. Biokhimiya 14, 86 (1949).
Formation and movement of enzymes in living organisms. Biokhimiya 16, 292 (1951).
Type of union of enzymes with the protein complex of plastids. Biokhimiya 17, 368 (1952).
Sizer, I. W.: Sucrose inversion by baker’s yeast as a function of temperature. J. Gen. Physiol. 21, 695 (1938).
Inactivation of invertase by tyrosinase. Science (Lancaster, Pa.) 108, 335 (1948).
Sosa-Bourdouil, C.: The enzymic activity of the antherozoids and the ovules of Fucus vesiculosus L. Bull. mus. nat. hist. nat. (Paris) 18, 142 (1946).
Enzymic activity of the inflorescences of Ginkgo biloba in the course of development. C. r. Acad. Sci. Paris 224, 1651 (1947).
Spiegelman, S., M. Sussman and B. Taylor: Isolation and characterization of two adaptive enzymes formed by yeast in response to maltose. Federat. Proc. 9, 120 (1950).
Stodola, F. H., H. J. Koepsell and E. S. Sharpe: A new disaccharide formed by Leuconostoc mesenteroides. J. Amer. Chem. Soc. 74, 3202 (1952).
Sumner, J. B., and S. F. Howell: Method for determination of saccharase activity. J. of Biol. Chem. 108, 51 (1935).
Sumner, J. B., and K. Myrbäck: The Enzymes. Chemistry and Mechanism of Action. New York: Academic Press 1950.
Sumner, J. B., u. D. J. O’Kane: The chemical nature of yeast saccharase. Enzymologia (Den Haag) 12, 251 (1948).
Takano, K., and T. Miwa: Enzymic transfer of glucose. II. Identity of glucotransferase and β-glucosidase. J. of Biochem. (Tokyo) 37, 435 (1950).
Enzymatic transfer of β-d-galactose. J. of Biochem. (Tokyo) 40, 471 (1953).
Takaoka, K.: The specific change of iodine reaction on sweet-potato starch caused by some microorganisms. II. The relation between the phenomenon and the amylolytic enzyme. J. Agric. Chem. Soc. Jap. 23, 390 (1950).
Thorsell, W., u. K. Myrbäck: Insoluble saccharase in baker’s yeast. Ark. Kemi (Stockh.) 3, 323 (1951).
Triff, I., and N. Dimofte: The effect of freezing on cigaret tobaccos. Bul. cultivar. fermentar. Tutunului 36, 79 (1947).
Veibel, S.: In: The Enzymes. Chemistry and Mechanism of Action. Edited by J. B. Sumner and K. Myrbäck. Vol. 1, Part. 1, p. 583 and p. 621. New York: Academic Press 1950.
Veibel, S., C. Møller u. J. Wangel: Investigations on the glycosidases of milk sugar yeast emulsin. Kgl. danske Vidensk. Selsk., Math.-fysiske Medd. 22, No 2 (1945).
Vintilescu, J., C. N. Ionescu u. A. Kizyk: Enzymatische Synthesen einiger α-Glukoside. Bul. Soc. Chim. Romania 17, 131 (1935).
Wallenfels, K., u. E. Bernt: Über die gruppenübertragende Wirkung von Disaccharidspaltenden Enzymen. Angew. Chem. 64, 28 (1952).
Wallenfels, K., E. Bernt u. G. Limberg: Isolierung von Lactotriose, Lactobiose und Galaktobiose aus dem enzymatischen Hydrolysat von Lactose. Liebigs Ann. 579, 113 (1953).
Wanner, H., u. U. Leupold: The longitudinal distribution of saccharase activity in the root tip. Ber. Schweiz. bot. Ges. 57, 156 (1947).
Weidenhagen, R.: Zur Frage der enzymatischen Rohrzuckerspaltung. Naturwiss. 16, 654 (1928).
Zur Frage der Saccharasespezifität. Z. Ver. dtsch. Zuckerind. 78, 406–418 (1928).
Die experimentellen Grundlagen der enzymatischen Rohrzuckerspaltung. Erg. Enzymforsch. 2, 90–103 (1933).
Weidenhagen, R., u. A. Renner: Über die Spezifität der Galaktosidase. Z. Ver. dtsch. Zuckerind. 86, 22–56 (1936).
Whelan, W. J., and D. M. Jones: β-Methyl fructoside as a substrate in transfructosylation. Biochemie. J. 54, XXXIV (1953).
White, J. W., and J. Mäher: Transglucosidation by honey invertase. Arch. of Biochem. a. Biophysics 42, 360 (1953).
α-Maltosyl β-d-fructofuranoside, a trisaccharide enzymatically synthesized from sucrose. J. Amer. Chem. Soc. 75, 1259 (1953).
White, L. M., and G. E. Secor: The oligosaccharides formed during the sucrose-invertase reaction. Arch. of Biochem. a. Biophysics 36, 490 (1952).
Wilkes, B. G., and E. T. Palmer: Similarity of the kinetics of invertase action in vivo and in vitro. II. J. Gen. Physiol. 16, 233 (1932).
Willstätter, R.: Untersuchungen über Enzyme. Berlin: Springer 1928.
Willstätter, R., u. E. Bamann: Trennung von Maltase und Saccharase. Hoppe-Seylers Z. 151, 273 (1926).
Willstätter, R., u. W. Grassmann: Freilegung des Invertins aus der Hefe. Biochem. Z. 203, 308 (1928).
Willstätter, R., u. R. Kuhn: Über Maßeinheiten der Enzyme. Ber. dtsch. chem. Ges. 56, 509 (1923).
Winge, Ö., u. C. Roberts: Relation between the polymeric genes for maltose, raffinose, and sucrose fermentation in yeasts. C. r. Labor. Carlsberg, Ser. Physiol. 25, 141–171 (1952).
Wolfrom, M. L., A.Thompson and T. T. Galkowski: 4-α-Isomaltopyranosyl-d-glucose. J. Amer. Chem. Soc. 73, 4093 (1951).
Wolochow, H., E. W. Ptttman, M. Doudoroff, W. Z. Hassid and H. A. Barker: Preparation of sucrose labeled with C14 in the glucose or fructose component. J. of Biol. Chem. 180, 1237 (1949).
Yasumura, A.: J. Jap. Biochem Soc. 26, 200 (1954).
Zechmeister, L., G. Tóth u. M. Bálint: Chromatographie separation of some of the enzymes of emulsin. Enzymologia (Den Haag) 5, 302 (1938).
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Gottschalk, A. (1958). The enzymes controlling hydrolytic, phosphorolytic and transfer reactions of the oligosaccharides. In: Åberg, B., et al. Aufbau · Speicherung · Mobilisierung und Umbildung der Kohlenhydrate / Formation · Storage · Mobilization and Transformation of Carbohydrates. Handbuch der Pflanzenphysiologie / Encyclopedia of Plant Physiology, vol 6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-94731-5_5
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