Characterization of a glycoprotein alpha-galactosidase from lentil seeds (Lens culinaris).

Dey, Prakash M.; Campillo, E M Del; Lezica, Rafael Pont

doi:10.1016/s0021-9258(18)33139-9

Cited by 43 publications

(5 citation statements)

References 41 publications

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“…The rate of the enzyme-catalyzed reaction increases to an optimum value with increasing temperature until inactivation of the enzyme occurs. Cicer α-galactosidase showed maximal activity at 50 °C (Figure ), and this optimum value is in good agreement with reported α-galactosidases from other sources. , The energy of activation ( E a ) was found to be 35.69 kJ/mol for Cicer α-galactosidase, similar to values reported from other sources ).…”

Section: Resultssupporting

confidence: 90%

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Purification and Characterization of α-Galactosidase from White Chickpea (Cicer arietinum)

Singh

Kayastha

2012

J. Agric. Food Chem.

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Glycosylated α-galactosidase (melibiase) has been purified from white chickpea ( Cicer arietinum ) to 340-fold with a specific activity of 61 units/mg. Cicer α-galactosidase showed a M(r) of 45 kDa on SDS-PAGE and by MALDI-TOF. The optimum pH and temperature with pNPGal were 4.5 and 50 °C, respectively. The K(m) for hydrolysis of pNPGal was 0.70 mM. Besides hydrolyzing the pNPGal, Cicer α-galactosidase also hydrolyzed natural substrates such as melibiose, raffinose, and stachyose very effectively; hence, it can be exploited commercially for improving the nutritional value of soy milk. Galactose was found to be a competitive inhibitor. The property of this enzyme to cleave the terminal galactose residues can be utilized for converting the group B erythrocytes to group O erythrocytes.

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Section: Resultssupporting

confidence: 90%

“…28,29 The energy of activation (E a ) was found to be 35.69 kJ/mol for Cicer α-galactosidase, similar to values reported from other sources. 35 Cicer α-galactosidase was quite stable at 50 °C, but at 70 °C it showed around 90% loss in activity (Figure 4).…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Purification and Characterization of α-Galactosidase from White Chickpea (Cicer arietinum)

Singh

Kayastha

2012

J. Agric. Food Chem.

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“…R-Galactosidases have been used for biotechnological purposes, including pretreatment of animal feed to hydrolyze nonmetabolizable sugars, thereby increasing the nutritive value (5), degradation of raffinose to improve the crystallization of sucrose (6), processing of soy molasses and soybean milk (7), improvement of the viscosity and gelling properties of galactomannan (8,9), stimulation of oil/gas wells through hydrolysis of the propant matrix (10), and conversion of B-type blood antigens to produce type O blood (11)(12)(13)(14). Because of their medical and technological importance, a number of R-galactosidases from eukaryotic and microbial sources have been studied (15)(16)(17)(18)(19).…”

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confidence: 99%

Biochemical Analysis of Thermotoga maritima GH36 α-Galactosidase (TmGalA) Confirms the Mechanistic Commonality of Clan GH-D Glycoside Hydrolases

et al. 2007

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Organization of glycoside hydrolase (GH) families into clans expands the utility of information on catalytic mechanisms of member enzymes. This issue was examined for GH27 and GH36 through biochemical analysis of GH36 alpha-galactosidase from Thermotoga maritima (TmGalA). Catalytic residues in TmGalA were inferred through structural homology with GH27 members to facilitate design of site-directed mutants. Product analysis confirmed that the wild type (WT) acted with retention of anomeric stereochemistry, analogous to GH27 enzymes. Conserved acidic residues were confirmed through kinetic analysis of D327G and D387G mutant enzymes, azide rescue, and determination of azide rescue products. Mutation of Asp327 to Gly resulted in a mutant that had a 200-800-fold lower catalytic rate on aryl galactosides relative to the WT enzyme. Azide rescue experiments using the D327G enzyme showed a 30-fold higher catalytic rate compared to without azide. Addition of azide to the reaction resulted in formation of azide beta-d-galactopyranoside, confirming Asp327 as the nucleophilic residue. The Asp387Gly mutation was 1500-fold catalytically slower than the WT enzyme on p-nitrophenyl alpha-d-galactopyranoside. Analysis at different pH values produced a bell-shaped curve of the WT enzyme, but D387G exhibited higher activity with increasing pH. Catalyzed reactions with the D387G mutant in the presence of azide resulted in formation of azide alpha-d-galactopryanoside as the product of a retaining mechanism. These results confirm that Asp387 is the acid/base residue of TmGalA. Furthermore, they show that the biochemical characteristics of GH36 TmGalA are closely related to GH27 enzymes, confirming the mechanistic commonality of clan GH-D members.

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“…α ‐Galactosidases have been identified across all kingdoms, including bacteria, fungi, marine Proteobacteria, and Bacteroidetes (Table 1). 5 Several isoforms of plant α ‐galactosidases belonging to the class GH 27, with varying functional pH and temperature optima, involved in the cleavage of terminal galactosyl residue from various complex structures have been described in legume seeds, vegetables, and ripening fruit tissue 41 . The enzyme also has a critical role in the physiological process of seed maturity and germination in crop plants, including annual yellow lupin ( Lupinus luteus ), 42 cowpea ( Vigna unguiculata ), 43 butter bean ( Phaseolus coccineus ), 44 cotyledons of pea ( Pisum sativum ), 7 soybean ( Glycine max ), 42 mountain coffee ( Coffea arabica ), 45 chickpea ( Cicer arientinum ), 46,47 muskmelon ( Cucumis melo ), 48 pumpkin ( Cucurbita pepo ), 48 barley ( Hordeum vulgar ), 48 ripening grape ( Vitis vinifera ), 49 and in the nectar of common tobacco ( Nicotiana tabacum ) 50 …”

Section: Production and Purification Of Omnipresent α‐Galactosidasementioning

confidence: 99%

Properties and applications of α‐galactosidase in agricultural waste processing and secondary agricultural process industries

Menon,

Pandurangan Maragatham,

Samuel

et al. 2023

J Sci Food Agric

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Agriculture products form the foundation building blocks of our daily lives. Although claimed to be dependent renewable resources with low carbon footprint, the agricultural community is constantly challenged to overcome two post‐harvest bottlenecks: one, the farm bio‐waste, a substantial economic and environmental burden to the farming sector, and second, an inefficient agricultural processing sector, plagued by the requirement of significant energy input to generate the products. Both these sectors require extensive processing technologies that are energy demanding and expensive. To address these issues, an enzyme(s)‐based green chemistry is available to break down complex structures into bio‐degradable compounds that source alternate energy with valuable by‐products and co‐products. Alpha‐galactosidase is a widespread class of glycoside hydroxylase that hydrolyzes alpha‐galactosyl moieties in simple and complex oligo and polysaccharides, glycolipids, glycoproteins. Owing to its growing importance, in this review we discuss the source of the enzyme, production and purification systems, and enzyme properties. We also elaborate on the enzyme's scope in agricultural bio‐waste management, secondary agricultural industries like sugar refining, soymilk derivatives, food and confectionery, and animal feed processing. Insight into this vital enzyme will provide new avenues for less expensive green chemistry‐based secondary agricultural processing and agricultural sustainability.This article is protected by copyright. All rights reserved.

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Characterization of a glycoprotein alpha-galactosidase from lentil seeds (Lens culinaris).

Cited by 43 publications

References 41 publications

Purification and Characterization of α-Galactosidase from White Chickpea (Cicer arietinum)

Purification and Characterization of α-Galactosidase from White Chickpea (Cicer arietinum)

Biochemical Analysis of Thermotoga maritima GH36 α-Galactosidase (TmGalA) Confirms the Mechanistic Commonality of Clan GH-D Glycoside Hydrolases

Properties and applications of α‐galactosidase in agricultural waste processing and secondary agricultural process industries

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