Development of α-galactosidase isoenzymes in chickpea seeds

Mittal, Yashoda; Sharma, Chitra

doi:10.1016/0168-9452(91)90087-o

Cited by 5 publications

(6 citation statements)

References 14 publications

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“…As well, the difference may be related to the bean preparation method. Soaking beans at room temperature prior to cooking as done by Acosta and Gross would initiate germination, which, in turn, initiates hydrolysis of galacto-oligosaccharides by α-galactosidase with possible liberation of free galactose …”

Section: Resultsmentioning

confidence: 99%

“…Soaking beans at room temperature prior to cooking as done by Acosta and Gross would initiate germination, which, in turn, initiates hydrolysis of galacto-oligosaccharides by αgalactosidase with possible liberation of free galactose. 47 In addition, the higher free galactose concentration found in the canning liquid indicates that the free galactose content associated with the consumption of canned legumes can be significantly reduced if the canning or cooking liquid is discarded and any residual liquid on the legumes is removed by rinsing.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Galactose Content of Legumes, Caseinates, and Some Hard Cheeses: Implications for Diet Treatment of Classic Galactosemia

Calcar

Bernstein

Rohr³

et al. 2014

J. Agric. Food Chem.

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There are inconsistent reports on the lactose and/or galactose content of some foods traditionally restricted from the diet for classic galactosemia. Therefore, samples of cheeses, caseinates, and canned black, pinto, kidney, and garbanzo beans were analyzed for free galactose content using HPLC with refractive index or pulsed amperometric detection. Galactose concentrations in several hard and aged cheeses and three mild/medium Cheddars, produced by smaller local dairies, was <10 mg/100 g sample compared to 55.4 mg/100 g sample in four sharp Cheddars produced by a multinational producer. Galactose in sodium and calcium caseinate ranged from undetectable to 95.5 mg/100 g sample. Free galactose level in garbanzo beans was lower than previously reported at 24.6 mg/100 g sample; black beans contained 5.3 mg/100 g, and free galactose was not detected in red kidney or pinto beans. These data provide a basis for recommending inclusion of legumes, caseinate-containing foods, and some aged hard cheeses that had been previously restricted in the diet for individuals with galactosemia.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Galactose Content of Legumes, Caseinates, and Some Hard Cheeses: Implications for Diet Treatment of Classic Galactosemia

Calcar

Bernstein

Rohr³

et al. 2014

J. Agric. Food Chem.

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“…In light of the identi®cation of SIPs as alkaline a-gals, representatives from at least ®ve plant families are now shown to have both alkaline and acid a-gals (Graminae (barley, SIP: M77475, acid: Y13848), Leguminoseae (Cicer, SIP: X95875, acid: Mittal and Sharma, 1991), Cucurbitaceae (melon, alkaline: this paper, acid: Solanaceae (tomato, SIP: TC94379, acid : Feurtado et al, 2001) and Cruciferae (Arabidopsis, SIPs: AAC83062, CAB66109, acid: CAB87430)). It is thus likely that the coexistence of both acid and alkaline a-gals will not be found to be an uncommon occurrence in the plant kingdom, analogous to the concomittant presence of acid and alkaline invertase.…”

Section: Discussionmentioning

confidence: 99%

Cloning and functional expression of alkaline α‐galactosidase from melon fruit: similarity to plant SIP proteins uncovers a novel family of plant glycosyl hydrolases

et al. 2003

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SummaryRaf®nose and stachyose are ubiquitous galactosyl-sucrose oligosaccharides in the plant kingdom which play major roles, second only to sucrose, in photoassimilate translocation and seed carbohydrate storage. These sugars are initially metabolised by a-galactosidases (a-gal). We report the cloning and functional expression of the ®rst genes, CmAGA1 and CmAGA2, encoding for plant a-gals with alkaline pH optima from melon fruit (Cucumis melo L.), a raf®nose and stachyose translocating species. The alkaline a-gal genes show very high sequence homology with a family of unde®ned`seed imbibition proteins' (SIPs) which are present in a wide range of plant families. In order to con®rm the function of SIP proteins, a representative SIP gene, from tomato, was expressed and shown to have alkaline a-gal activity. Phylogenetic analysis based on amino acid sequences shows that the family of alkaline a-gals shares little homology with the known prokaryotic and eukaryotic a-gals of glycosyl hydrolase families 27 and 36, with the exception of two cross-family conserved sequences containing aspartates which probably function in the catalytic step. This previously uncharacterised, plant-speci®c a-gal family of glycosyl hydrolases, with optimal activity at neutral-alkaline pH likely functions in key processes of galactosyl-oligosaccharide metabolism, such as during seed germination and translocation of RFO photosynthate.

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“…In recent years, many α-galactosidases have been extracted and purified from various sources. In plants, α-galactosidases are maximally distributed in seeds, fruits and leaves [7,8,9,10]. In microorganisms, α-galactosidases have been purified from the bacterium Flavobacterium sp.…”

Section: Introductionmentioning

confidence: 99%

A Fungal α-Galactosidase from Tricholoma matsutake with Broad Substrate Specificity and Good Hydrolytic Activity on Raffinose Family Oligosaccharides

et al. 2015

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An acidic α-galactosidase designated as TMG was purified from the fruiting bodies The purification protocol entailed ion exchange chromatography on Q-Sepharose and of Tricholoma matsutake with 136-fold purification and a specific activity of 909 units/mg. Mono-Q and fast protein liquid chromatography on Superdex 75. TMG is a monomeric protein exhibiting a molecular mass of 47 kDa in SDS-PAGE and gel filtration. The purified enzyme was identified by LC-MS/MS and three inner amino acid sequences were obtained. The optimum pH and temperature for TMG with pNPGal as substrate were pH 4.5 and 55 °C, respectively. The α-galactosidase activity was strongly inhibited by K

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Development of α-galactosidase isoenzymes in chickpea seeds

Cited by 5 publications

References 14 publications

Galactose Content of Legumes, Caseinates, and Some Hard Cheeses: Implications for Diet Treatment of Classic Galactosemia

Galactose Content of Legumes, Caseinates, and Some Hard Cheeses: Implications for Diet Treatment of Classic Galactosemia

Cloning and functional expression of alkaline α‐galactosidase from melon fruit: similarity to plant SIP proteins uncovers a novel family of plant glycosyl hydrolases

A Fungal α-Galactosidase from Tricholoma matsutake with Broad Substrate Specificity and Good Hydrolytic Activity on Raffinose Family Oligosaccharides

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