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  • 1
    Electronic Resource
    Electronic Resource
    Changes in Texture and Cell Wall Polysaccharides of Olive Fruit during "Spanish Green Olive" Processing (1995)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 43 (1995), S. 2240-2246 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf00056a051
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  • 2
    Electronic Resource
    Electronic Resource
    Activity of cell wall-associated enzymes in ripening olive fruit (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 93 (1995), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Enzymatically active cell wall isolaled from olive (Olea europaea) fruit was employed Hi investigate some hydrolytic enzymes bound to the cell wall and the changes in these during ripening. Seven glycosidases. β-glucosidase (EC 3.2.1.21) α-galactosidase (EC 3.2.1.22). β-galactosidase (EC 3.2.1.23). α-arabinosidase (EC 3.2.1.55), α-mannosidase (EC 3.2.1,24). β-xylosidase (EC 3.2.1.37) and β-N-acetylglucosamidase (EC 3.2.1.30). as well as Cx-cellulase (EC 3.2.1.4) and endo-polygalacturonase (EC 3.2.1.15). were identified in the cell wall preparation, at four stages of ripeness (mature green. changing colour, black and black-ripe). Activities of all these cell wall-associated enzymes fionicallv and covalently linked) were determined either by cell wall incubation with artificial substrate or after extraction from the cell wall with buffers of high salt concentration (Cx-cellulase). and were compared to those of forms solubilized from acetone powders with 500 nM citrate buffer (cytoplasmic and/or apoplastic plus ionically hound to cell wall) In general, the activities of low ionic strength buffer-soluble enzymes were found to be much higher than those of the bound enzymes. The bound enzymes are present in the fruit at the green colour stage, whereas the activities of the soluble enzymes only increased from the changing colour stage onwards. The tenacity of binding of enzymes to the wall was investigated by treating the walls with high salt and measuring residual activity. The nature of the ionic and covalent binding and the changes during ripening were also established for wall-hound glycosidase During ripening there was a marked change in the percentages of covalently- and tonically linked activities of β-glucosidase and β-galaclosidase: al the changing colour stages about 75–80% of the bound active in was present in high ionic strength buffer while al the black-ripe stage it was only 15–20. A possible role for these cell wall degradative enzymes in olive softening is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1995.tb05113.x
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  • 3
    Electronic Resource
    Electronic Resource
    Cell Wall Composition of Olives (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 59 (1994), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cell walls of olives (Olea europaea L.), Hojiblanca and Manzanilla, were isolated and fractionated into polysaccharides, and compositions compared. Pectic and hemicellulosic fractions were purified by ion exchange and gel filtration chromatography, and neutral sugar and uronic acid composition determined. Differences occurred between cultivars and seasons: Manzanilla had higher pectic polysaccharides and lower xylans. Hojiblanca showed similar but lesser differences. Arabinans were the main neutral pectic polysaccharides with arabinose 〉 80%. Homogalacturonans and rhamnogalacturonans were 〉 50% of the acidic pectic fractions. Degree of esterification and molecular weights were related to extracting solvent. Xyloglucans and galactoglucomannans were neutral hemicelluloses with molecular weights ≅ 260 kD. Glucuronoarabinoxylans had higher molecular weights (up to 400 kD). Acidic xylans were important in the pulp.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1994.tb14674.x
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  • 4
    Electronic Resource
    Electronic Resource
    Changes in cell-wall-degrading enzyme activities in stored olives in relation to respiration and ethylene production Influence of exogenous ethylene (1997)
    Springer
    Zeitschrift für Lebensmittel-Untersuchung und -Forschung 204 (1997), S. 293-299 
    Details
    ISSN: 1431-4630
    Keywords: Key words Olives ; Cell wall ; Enzymes ; Ethylene ; Storage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The activity of various enzymes (α-D-galactosidase; β-D-galactosidase; α-L-arabinofuranosidase; α-D-mannosidase, β-D-N-acetylglucosaminidase, cellulase and polygalacturonase) associated with the cell wall during olive storage was assayed in order to establish the behaviour of the enzymes as a function of the ripening stage and in relation to the production of ethylene. The effect of exogenous ethylene (100 mg/l for 24 h) was also evaluated. In addition, gaseous emissions of CO2 and ethylene during olive storage were monitored. The results obtained indicate that the high initial CO2 level in the green olive coincides almost exactly in time with the climacteric maxima when the fruit is on the tree. After the rapid decrease in the respiration rate of green olives during storage, the CO2 production rate increases as the stage of maturity advances. The results also indicate that ethylene is not capable of stimulating the activity or synthesis of enzymes in green olives, but can produce such a stimulation in black olives. Furthermore, during the first day of storage there were very marked decreases in enzyme activities. Small variations in the conditions of aerobiosis in post-harvest ripening were shown to have notable effects on the normal metabolism of the fruits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002170050080
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  • 5
    Electronic Resource
    Electronic Resource
    Cellulases in cell wall-degrading extracts ofOlea europaea arolensis (1990)
    Springer
    European food research and technology 190 (1990), S. 22-24 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Description / Table of Contents: Summary In this report the considerable increase in cellulases activity of olive fruits (Olea europaea arolenis) during ripening and softening has been studied. Ethylene is shown as the initiating agent of this activity. Some characteristics of these enzymes, such as the linear relationship between intrinsic viscosity/incubation time and between cellulolytic activity/enzyme concentration, are established. The cellulase, which is stable up to 50°C, presents maximum activity at pH 5.7
    Notes: Zusammenfassung In dieser Arbeit wird die erhebliche Steigerung der Cellulasen-Aktivität in den Olivenfrüchten (Olea europaea arolensis) während der Reifung und des Weichwerdens studiert. Ethylen ist der Initiator dieser Aktivität. Einige dieser Enzyme sind verantwortlich für die lineare Beziehung zwischen der wirklichen Viscosität und der Incubationszeit und zwischen der cellulytischen Aktivität und der Enzymkonzentration. Die Cellulase ist stabil bis 50°C bei einem pH-Wert von 5,7.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01188258
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  • 6
    Electronic Resource
    Electronic Resource
    Inhibitors of cellulolytic activity in olive fruits (Olea europaea, Hojiblanca var.) (1990)
    Springer
    European food research and technology 190 (1990), S. 232-232 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01192972
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  • 7
    Electronic Resource
    Electronic Resource
    Evolution of endoglucanase activity in olives during ripening and storage and its relationship with cellulolytic microorganisms (1992)
    Springer
    European food research and technology 195 (1992), S. 451-454 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Description / Table of Contents: Summary Cellulolytic enzymes are responsible for many of the changes associated with the ripening process in olive fruits (Olea europaea). Evolution of endoglucanase activity (EC 3.2.1.4.) was studied in olives during their ripening and softening, both on the tree and after being picked and stored, and was related to the presence of microorganisms. The time course of cellulolytic activity was measured for four stages of ripeness (green, turning colour, black and ripe black) and was related to the total number of cellulolytic bacteria. The increases in activity during ripening and storage gave an indication of how normal flora influences during the olive ripening process.
    Notes: Zusammenfassung Die cellulolytischenEnzyme sind für viele Veränderungen während des Reifens der Olive verantwortlich. Es wurde daher die Aktivität der Enzyme während der Entwicklung der Olive bei der Reifung und dem Weichwerden studiert, und zwar am Baum, nach der Ernte und nach dem Lagern, was auch in Beziehung zu der Gegenwart von Mikroorganismen steht. Es wurde die cellulolytische Aktivitätsentwicklung während der vier Reife-Zustände (grün, farbenwechselnd, schwarz und zartes schwarz) studiert und auf die Gesamtzahl der cellulolytischen Bakterien bezogen. Der Aktivitäts-Zuwachs während des Reifens und Lagerns gibt einen Hinweis, wie die normale Flora auf das Reifen der Oliven einwirkt.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01191716
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  • 8
    Electronic Resource
    Electronic Resource
    Activity of glycosidases during development and ripening of olive fruit (1993)
    Springer
    European food research and technology 196 (1993), S. 147-151 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Description / Table of Contents: Summary We have studied the activity of variousp-nitrophenyl-d-glycosidases during development and ripening of olive fruit in three seasons (1987–88, 1988–89, 1989–90). Activity was absent in the first phases of ripening but appeared in the completely developed fruit,α-Galactosidase,β-galactosidase,α-mannosidase,α-arabinosidase, andα-xylosidase activities were detected and their relative molecular mass determined by gel filtration chromatography using Sephadex G-100. There is a temporal correlation between enzymatic activity and decrease in non-cellulosic cell-wall neutral sugar composition.
    Notes: Zusammenfassung Es wurde die Aktivität von verschiedenenp-Nitrophenyl-d-glycosidasen während der Entwicklung und Reifung der Oliven in drei Jahren (1987–88; 1988–89, 1989–90) untersucht. Es wurde keine Aktivität in der voll entwickelten Frucht festgestellt. Es wurden die Aktivitätenα-Galactosidase,β-Galactosidase,α-Mannosidase,α-Arabinosidase undα-Xylosidase entdeckt und ihre Molekularmassen durch Gelfiltration-Chromatographie mit Sephadex G-100 bestimmt. Es gibt eine zeitliche Wechselwirkung zwischen der enzymatischen Aktivität und der Abnahme in der Zuckerzusammensetzung in dem Nichtcellulose-Anteil der Zellwand.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01185575
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  • 9
    Electronic Resource
    Electronic Resource
    Olive fruit glycosidases: factors affecting their extraction (1992)
    Springer
    European food research and technology 194 (1992), S. 561-565 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Description / Table of Contents: Summary The enzymes α- and β-galactosidase, α-mannosidase, and α-arabinosidase have been detected in olives during the process of development and ripening. The extraction of enzymes can be achieved at low ionic strength of the medium, which shows that these are not associated with the cell wall. High concentrations of salt strongly inhibited all the enzymes. Consistent determination of activity can be done using thep-nitrophenyl method without appreciable interference below a control absorbance of 0.8 units. However, significant interference was found above this value. The apparent optimum pH for the four enzymes was between 4.3 and 5.3 units. The optimum temperature for a incubation time of 15 min was 50 and 60° for α- and β-galactosidase, and 40 and 50°C for α-mannosidase and α-arabinosidase. The respective activation energies were estimated. All the enzymes possess a relativelyl high thermal stability, αmannosidase and β-galactosidase being slightly more stable than α-galactosidase and α-arabinosidase.
    Notes: Zusammenfassung Die Enzymeα- undβ-Galaktosidase, α-Mannosidase und α-Arabinosidase wurden während der Entwicklung und Reifung der Oliven entdeckt. Die Extraktion der Enzyme wird bei niederer lonenstärke erreicht, was belegt, daß diese nicht mit der Zellwand verbunden sind. Hohe Salzkonzentrationen hemmen diese Enzyme stark. Aktivitätsbestimmungen können mit derp-Nitrophenyl-Methode ohne wesentliche Interferenzen bis unter die Kontrollabsorption von 0,8 Einheiten durchgeführt werden; jedoch wurden signifikante Unterschiede über diesen Wert gefunden. Der optimale pHWert für diese vier Enzyme war zwischen 4,3 und 5,3 Einheiten. Die optimale Temperatur bei einer Bebrütungszeit von 15 min war 50–60°C für die α- und β-Galaktosidase und 40–50°C für die α-Mannosidase und αArabinosidase. Die jeweiligen Aktivierungsenergien wurden ebenfalls bestimmt. Alle Enzyme besitzen eine relativ hohe thermische Stabilität, wobei die α-Mannosidase und die β-Galaktosidase etwas stabiler als die α-Galaktosidase und die α-Arabinosidase sind.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01185484
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  • 10
    Electronic Resource
    Electronic Resource
    Identification of endoglucanases in olives (Olea europaea arolensis) (1991)
    Springer
    European food research and technology 193 (1991), S. 554-557 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Description / Table of Contents: Summary A knowledge of the ripening and softening processes of olives is extremely interesting for Spain since it is the principal producer in the industry of olive preparations for the table. Cellulolytic activity has been detected in this fruit with an increase of cellulase concentration during the various stages of the vegetative cycle; this has an important influence on ripening. Three enzymatic forms appear: endoglucanases, exoglucanases andβ-glucosidase; this study deals with the identification and partial characterization of endoglucanases. The existence of an endoglucanase with different eight apparently molecular forms has been suggested by gel filtration, ion exchange chromatography and electrophoresis.
    Notes: Zusammenfassung Die Kenntnisse über das Reifen und Erweichen der Olive sind für Spanien sehr wichtig, weil es das Hauptland für die industrielle Bearbeitung der Speisenoliven ist. Man hat Cellulase-Aktivität nachgewiesen, die sich während der weiteren Entwicklungsstadien vergrößerte. Dieser Cellulasen-Zuwachs hat einen wichtigen Einfluß auf das Reifen und Weichwerden. Von den drei Enzymformen der Endoglucanase, der Exoglucanase und derβ-Glucosidase beschäftigt sich diese Arbeit nur mit der ersteren. Das Vorkommen der Endoglucanase mit acht Untereinheiten, mit den Molekulargewichten 72,000; 59,000; 51,000; 48,000; 44,000; 32,000; 23,000 und 18,000 konnte durch Gelfiltration, Chromatographie, Ionenaustausch und Elektrophorese nachgewiesen werden.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01190872
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