Optimization, production and partial purification of βglucosidase from yeast using citrus peel
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Date
2016
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Punjab Agricultural University, Ludhiana
Abstract
The enzyme β-glucosidase hydrolyzes cellobiose and short chain cello-oligosaccharides to
glucose. The study was conducted to evaluate the production of enzyme β-glucosidase using
economically viable substrate citrus fruit waste with optimized batch scale fermentation using
Clavispora lusitaniae strains KF633446 and KP131848.1 as yeast inoculum. The process
parameters optimized during study are: substrate concentration (117.9g/L lemon peel powder
or 46.875 g/L lime) or 16.8 g/L banana peel powder, temperature (35°C) and pH (5) ,
inoculum concentration of 0.75% v/v, time period of 36 h and 30h using yeast strains
KP131848.1 and KF633446 respectively. Use of citrus fruit waste as substrate for enzyme
production has proved to be economical; the maximum enzyme activity 0.49 IU/ml with
lemon peel, followed by lime (0.28 IU/ml) and banana peel (0.337 IU/ml). The enzyme
activity (IU) of β-glucosidase after partial purification was found to be 18.52 IU. The partially
purified β-glucosidase was highly stable at temperature 45°C and pH 5. The value of Km and
Vmax was 1.25mM and 17.98 IU/ml respectively using pNPG (para-nitrophenyl-β-Dglucopyranoside)
as substrate. The addition of enzyme @ 0.4 ml per 100 ml of juice resulted
in increased reducing sugar content in sweet lime juice (58.42%), grapefruit juice (57.36%),
lemon juice (55.26%) and kinnow juice (53.19%), with storage time period of 15 days.
Sensory analysis on 9 point hedonic scale revealed maximum score of 8.4±0.2 for aroma and
7.85±0.25 for flavour of lemon juice. This study revealed the commercial utilization of peel
as substrate for β-glucosidase production and wide applicability of β-glucosidase enzyme in
aroma and flavor enhancement along with debittering properties of enzyme Naringinase and
Limonin dehydrogenase.
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