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1.
J Biosci ; 1988 Mar; 13(1): 33-38
Article in English | IMSEAR | ID: sea-160633

ABSTRACT

The potentiality of apple cell cultures to synthesize not only higher quantities of lipids than apple fruit but also different classes of lipids is noted. Total lipid was 15-fold higher in apple callus than in the original tissue. On callusing, linoleic acid decreased from 66% to 14%, while linolenic acid showed a very large increase from 0·9% to 44%. Stearic and oleic acids also increased in callus. The relative amounts of sterol/hydrocarbon and diglyceride fractions were higher in callus cultures, while apple tissue showed higher levels of triglycerides and sterol. Phosphatidylethanolamine and phosphatidylglycerol seemed to be newly synthesized during callusing while other phospholipids such as lysophosphatidylcholine, lysophosphatidylethanolamine, phosphatidylinositol and phosphatidic acid decreased. There was much higher glycolipid in apple callus than in the original tissue. The ratio of neutral lipid to polar lipid was higher in apple than in apple callus.

2.
Indian J Biochem Biophys ; 1983 Oct; 20(5): 311-4
Article in English | IMSEAR | ID: sea-26480

Subject(s)
Acids , Fruit
3.
J Biosci ; 1982 Dec; 4(4): 401-403
Article in English | IMSEAR | ID: sea-160175

ABSTRACT

Thin layer chromatographic separation of chloroform-methanol extracts of mango on silica gel revealed a fluorescent substance in mango peel and pulp. The compound had fluorescence spectrum similar to that of lipofuscin, the age pigment of animal tissues and was found to be water insoluble and stable to ultraviolet irradiation. The fluorescent material appeared to be a lipoprotein.

4.
J Biosci ; 1982 Mar; 4(1): 69-78
Article in English | IMSEAR | ID: sea-160115

ABSTRACT

Polyphenoloxidase from mango (Mangifera indica) peel was purified to homogeneity by ammonium sulphate fractionation, chromatography on DEAE-Sephadex and gel filtration of Sephadex G-200. The enzyme had an apparent molecular weight of 136,000. Its pH and temperature optimum were 5.4 and 50°C, respectively. The enzyme possessed catecholase activity and was specific to o-dihydroxy phenols. The enzyme also exhibited peroxidase activity. Some non-oxidizable phenolic compounds inhibited the enzyme competitively. High inhibitory effects were also shown by some metal chelators and reducing agents, Mango peel polyphenol oxidase when immobilized onto DEAE Sephadex showed slightly higher Km for catechol and lower pH and temperature optima.

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