Limonin Bitterness in Citrus Juices

Hasegawa, Shin

doi:10.1007/978-1-4615-4693-1_9

Cited by 8 publications

(6 citation statements)

References 74 publications

(73 reference statements)

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“…[21] Lime residue samples contained significant level of pectin and the values obtained were similar to those previously reported in lemon pulp (22.53 g=100 g dry basis) and sweet orange peels (23.02 g=100 g, dry basis) [5] and higher than the by-products from lemon (7.5 g=100 g, dry basis), orange (6.5 g=100 g, dry basis), and grapefruit (3.5 g=100 g, dry basis). [1] Naturally, limonin in all citrus fruit tissues [22] and the amounts are varied greatly depending on the variety and part of the fruit. [23,24] Limonin content in lime residues was observed to be higher than that reported in Citrus changshanensis.…”

Section: Effect Of Blanching On Chemical Compositionsmentioning

confidence: 99%

Effects of Pretreatment and Drying on Composition and Bitterness of High-Dietary-Fiber Powder from Lime Residues

2009

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Lime residues after juice extraction were used as a starting raw material to produce high-dietary-fiber powder. The effects of pretreatment-i.e., blanching and ethanol soaking (55-95% v/v)-and hot air drying at 60-100 C on the proximate composition and limonin, a substance responsible for bitterness in citrus fruits, were evaluated. Hydration properties-i.e., water retention capacity and swelling capacity-and visual color were also determined. It was found that using selected pretreatments in combination with the drying process caused significant effects on dietary fiber contents and visual color. The higher reduction in limonin contents was observed for the samples having subjected to higher ethanol concentration and higher drying temperature. Blanching and ethanolic pretreatment also improved the water retention and swelling properties of the final product.

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Section: Effect Of Blanching On Chemical Compositionsmentioning

confidence: 99%

Effects of Pretreatment and Drying on Composition and Bitterness of High-Dietary-Fiber Powder from Lime Residues

2009

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“…Citrus tissues possess naringin, a flavonoid responsible for the bitter taste (Hasegawa & Maier 1993). Different approaches have been used to avoid naringin bitterness or to eliminate this flavonoid from citrus juices but few have achieved significant success (Johnson & Chandler 1988;Kimball 1991).…”

Section: Introductionmentioning

confidence: 98%

Purification and characterization of naringinase from a newly isolated strain of Aspergillus niger 1344 for the transformation of flavonoids

Puri

Kalra

2005

World J Microbiol Biotechnol

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An extracellular naringinase (an enzyme complex consisting of a-L-rhamnosidase and b-D-glucosidase activity, EC 3.2.1.40) that hydrolyses naringin (a trihydroxy flavonoid) for the production of rhamnose and glucose was purified from the culture filtrate of Aspergillus niger 1344. The enzyme was purified 38-fold by ammonium sulphate precipitation, ion exchange and gel filtration chromatography with an overall recovery of 19% with a specific activity of 867 units per mg of protein. The molecular mass of the purified enzyme was estimated to be about 168 kDa by gel filtration chromatography on a Sephadex G-200 column and the molecular mass of the subunits was estimated to be 85 kDa by sodium dodecyl sulphate-Polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme had an optimum pH of 4.0 and temperature of 50°C, respectively. The naringinase was stable at 37°C for 72 h, whereas at 40°C the enzyme showed 50% inactivation after 96 h of incubation. Hg 2+ , SDS, p-chloromercuribenzoate, Cu 2+ and Mn 2+ completely inhibited the enzyme activity at a concentration of 2.5-10 mM, whereas, Ca 2+ , Co 2+ and Mg 2+ showed very little inactivation even at high concentrations (10-100 mM). The enzyme activity was strongly inhibited by rhamnose, the end product of naringin hydrolysis. The enzyme activity was accelerated by Mg 2+ and remained stable for one year after storage at )20°C. The purified enzyme preparation successfully hydrolysed naringin and rutin, but not hesperidin.

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“…Naringin is the source of undesirable bitterness especially in citrus fruit juice industry; therefore, it must be removed or reduced its levels from the processed products (Yusof et al 1990; Hasegawa and Maier 1993). This bitter taste was decreased by the reduction of naringin content which was carried out using chemical methods, but this method had several drawbacks resulting in the inferior quality of fruit juice (Puri et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin

et al. 2016

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Naringinase induced from the fermented broth of marine-derived fungus Aspergillus niger was immobilized into grafted gel beads, to obtain biocatalytically active beads. The support for enzyme immobilization was characterized by ART-FTIR and TGA techniques. TGA revealed a significant improvement in the grafted gel’s thermal stability from 200 to 300 °C. Optimization of the enzyme loading capacity increased gradually by 28-fold from 32 U/g gel to 899 U/g gel beads, retaining 99 % of the enzyme immobilization efficiency and 88 % of the immobilization yield. The immobilization process highly improved the enzyme’s thermal stability from 50 to 70 °C, which is favored in food industries, and reusability test retained 100 % of the immobilized enzyme activity after 20 cycles. These results are very useful on the marketing and industrial levels.

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Limonin Bitterness in Citrus Juices

Cited by 8 publications

References 74 publications

Effects of Pretreatment and Drying on Composition and Bitterness of High-Dietary-Fiber Powder from Lime Residues

Effects of Pretreatment and Drying on Composition and Bitterness of High-Dietary-Fiber Powder from Lime Residues

Purification and characterization of naringinase from a newly isolated strain of Aspergillus niger 1344 for the transformation of flavonoids

Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin

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