Bookcover of Improvement Of Lycopene Extraction With Partially Purified Enzymes

Improvement Of Lycopene Extraction With Partially Purified Enzymes

LAP LAMBERT Academic Publishing (2013-05-11 )

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Lycopene is the carotenoid which gives tomatoes and other red fruits their characteristic colour. It is one of the most powerful antioxidants and singlet oxygen-quenching agents. Lycopene has been found to be of great medical importance, having various anticancer effects and it is able to ameliorate several other medical conditions. Lycopene had also been found to be very useful in the food industry where it is used as food additives, colourant and functional food. Lycopene, has been the focus of considerable attention for its potential health benefits (Shi et al. 2002; Rao and Rao, 2004). Results from epidemiological and experimental studies support the view that lycopene may provide protection against cardiovascular disease and certain types of cancer (Giovannucci, 2005; Omoni and Aluko, 2005). Lavecchia and Zuorro (2011) reported the growing demand for natural lycopene and therefore considerable interest has been directed to the possibility of obtaining lycopene from tomato processing waste. This growing demand for natural lycopene has led us to device an alternative means for the extraction of lycopene using enzymes.
Publishing house:
LAP LAMBERT Academic Publishing
By (author) :
Oluwabunmi Adedeji, Adesola Ajayi
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49.90 €
Enzymes, Aspergillus niger, Lycopene, Cellulase, Polygalacturonase

Price 49.90 €
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1 - 5 / 8
  • More InfoStudies on Polygalacturonase Production from Isolated BacillusC4
  • More InfoGlycoside Hydrolase Family 28
  • More InfoGene Cloning and Construction of Expression Vector
  • More InfoRole of Polygalacturonases in Fruit Ripening Process
  • More InfoBiochemical Studies of Alternaria blight of cluster bean
  • More InfoAdding value to the citrus pulp by enzyme biotechnology production
  • More InfoFructooligosaccharides
  • More InfoBioinformatics analyses of Eukaryotic mRNAs and Industrial Enzymes


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Studies on Polygalacturonase Production from Isolated BacillusC4


The present investigation is envisaged to study the production of alkaline and thermostable polygalacturonase using isolated soil Bacillus subtilis(C4) by submerged fermentation. A total of 66 bacterial colonies were isolated from six sampling sites. Out of 66 isolates 8 isolates showed polygalacturonase activity and C4 isolate showed maximum activity. The new isolate polygalacturonase potential was tested against three polygalacturonase producing microorganism. Comparatively isolate C4 showed maximum enzyme activity hence it was chosen for in depth study. The isolate C4 was characterized and identified as Bacillus subtilis C4. The new Bacillus subtilis was used for polygalacturonase production under submerged ferementation Growth profile of the above isolate was studied. The results revealed that the organism was showing maximum log phase till 24hr period after which the growth gradually reduced and remained stable till 72h indicating stationary phase at 400C and pH 11.0. Process parameters like incubation time (19.65U/mL), temperature (28.08 U/mL),pH 7.0, inoculum volume(1mL), inoculum age (24h) and agitation (150rpm) were studied for maximum production of polygacturonase.

Glycoside Hydrolase Family 28


Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. In molecular biology, glycoside hydrolase family 28 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy( web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.

Gene Cloning and Construction of Expression Vector


Polygalacturonase one of the hydrolytic enzymes involved in the degradation of pectin and cellulose content of the growing tissues in many horticultural plants. CaPG gene is responsible for the production of polygalacturonase in capsicum cultivars, under laid project is associated with the cloning of CaPG gene and construction of many appropriate vectors carries the aim gene in bacteria and other interested commodities. Expression vector termed as pVBG2307 is unique and novel vector offering more broader cloning site with greater than twenty restriction endonucleases.

Role of Polygalacturonases in Fruit Ripening Process


Ripening is a dramatic event in the physiology of a fruit. It is visualised by monitoring changes in color, smell and texture of the fruit. Among these, change in texture is an important aspect as it has a great impact on the life of the fruit. Textural changes are effected by various pectolytic enzymes, each one having a characteristic role in individual fruits. The pectinesterases have been intensively studied in almost all fruits and vegetables. The polygalacturonases have been relatively less studied. Hence, the book emphasises on the presence and role of polygalacturonase in fruit ripening. It is hoped that the information contained herein will provide - insights to biochemists, especially protein biologists, vital information to biotechnologists specializing in molecular biology and even food technologists.

Biochemical Studies of Alternaria blight of cluster bean


There was significant increase in peroxidase (PO), polyphenol oxidase (PPO) and phenylalanine ammonia lyase (PAL) activities in diseased leaves of all three varieties-RGC-936 (susceptible), RGC-1003 (moderately resistant) and RGC-986 (resistant) of clusterbean. Significant decrease in catalase activity was observed in diseased leaves than healthy ones and this decrease was more pronounced in susceptible variety RGC-936.The pathogen related enzymes polygalacturonase trans-eliminase (PGTE), pectin trans-eliminase (PME), polygalacturonase (PG) and cellulolytic (Cx) enzymes activities were found lower at initial stages of observations.The soluble protein content in healthy leaves of RGC-986 was highest followed by RGC-1003 while, it was lowest in RGC-936. It was significantly decreased in diseased leaves of all three varieties. Maximum decrease in soluble protein “due to infection” was observed in RGC-936 followed by RGC- 986 and RGC-1003.Total phenolic contents were higher in healthy leaves of RGC-986 followed by RGC-1003 and RGC-936.

Adding value to the citrus pulp by enzyme biotechnology production


The citrus pulp obtained from orange (Citrus sinensis) in industrial process is an important residue in countries where orange juice is produced. Enzyme production from this waste can reduce costs of biotechnological processes for the production of food and bioenergy since this residue is not expensive. In this book the citrus pulp was evaluated as substrate for the production of polygalacturonases, cellulases, reduced sugars, and protein for feed by Trichoderma reesei or Aspergillus niger in a cell recycle Batch process. The crude protein in the solid residue after this culture was also evaluated. Good levels of enzymes and protein enrichment of this residue are possible to obtain with the proposed technology.



Fructooligosaccharides (FOS) are short-chain fructans with a terminal glucose moiety and are found naturally in many plant species. Besides their wide use as an alternative sweetener in food and beverage industry, FOS have shown great potential as neutraceuticals against diabetes, colon cancer and bowel disease. The uses of FOS are dependent on the degree of polymerisation that they exhibit. In this study, fructosyltransferase (FTase) and polygalacturonase (PGase) activities, present in a commercial enzyme preparation (Pectinex®Ultra SP-L) sourced from Aspergillus aculeatus, have been separated and fully purified by anion-exchange and size-exclusion chromatography. The FTase possesses fructosyl transfer activity for FOS synthesis and the PGase has pectin hydrolytic activity. Analysis of various mixtures of FOS by mass spectrometry, HPLC and 1H-NMR was undertaken. Results indicated that MS with electrospray ioniza-tion and 1H-NMR are capable of providing relative quantitative data of the FOS present in the mixtures.

Bioinformatics analyses of Eukaryotic mRNAs and Industrial Enzymes


Bioinformatics programmes and genetic engineering techniques have become powerful tools to understand structure-function relationships of macromolecules. This monograph deals with the analyses of proteins and nucleic acids using these tools. The first paper describes development of a new software to analyze the untranslated regions in eukaryotic mRNAs. UTRScan utility has been used to analyze these regions (cis acting elements) in mRNAs. However, the UTRScan is not very sensitive and also not highly specific. We have developed a new algorithm and an Internet based web application tool named UlTRaSCAN, which overcomes these limitations and proved to be highly specific and sensitive in detecting patterns in UTRs. The second paper describes an anomaly observed in the commonly used multiple sequence analysis programmes viz., ClustalW and T-COFFEE. The third and fourth papers combine the knowledge of biochemical and genetic engineering data with bioinformatics data to analyze active sites of enzymes such as polygalacturonases, invertases and fructofuranosyl transferases. I do hope these articles will make an interesting reading not only for the specialists but also for the beginners.