Dioscorin, the Major Tuber Storage Protein of Yam (<i>Dioscorea batatas </i>Decne) with Carbonic Anhydrase and Trypsin Inhibitor Activities

Hou, Wen Chi; Liu, Jih Shiou; Chen, Hsien-Jung; Chen, Tzeng Err; Chang, Chun-Hung; Lin, Yaw Huei

doi:10.1021/jf980738o

Cited by 75 publications

(54 citation statements)

References 29 publications

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“…Hou et al (33,34) claimed that dioscorins from D. batatas showed both carbonic anhydrase and trypsin inhibitory activities by activity staining on SDS-PAGE. However, it should be mentioned that the activities could be detected even after 2-mercaptoethanol treatment and the carbonic anhydrase activity was zinc-independent.…”

Section: Purification and Subunit Structures Of Tubermentioning

confidence: 99%

Characterization of the Yam Tuber Storage Proteins from Dioscorea batatas Exhibiting Unique Lectin Activities

Gaidamashvili¹,

Ohizumi

Iijima

et al. 2004

Journal of Biological Chemistry

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Four major proteins designated DB1, DB2, DB3, and DB4 were isolated and characterized from the yam tuber Dioscorea batatas. The ratios of their yields were 20:50:20:10. DB1 was a mannose-binding lectin (20 kDa) consisting of 10-kDa subunits and was classified as the monocot mannose-binding lectin family. DB2, accounting for 50% of the total protein, was the storage protein, commonly called dioscorins consisting of a 31-kDa subunit. On the basis of amino acid sequence, DB2 was classified to be dioscorin A. DB3 was a maltose-binding lectin, having an apparent molecular mass of 120 kDa and composed of a 66-kDa subunit and two 31-kDa subunits (DB3S). The 66-kDa subunit was further composed of two 31-kDa subunits (DB3L) cross-linked by disulfide bonds. DB3L and DB3S (242 and 241 amino acid residues, respectively) were homologous with each other with 72% sequence identity. They showed a sequence homology to dioscorin B and dioscorin A from Dioscorea alata, with 90 and 93% identity, respectively, and to carbonic anhydrase from Arabidopsis thaliana with about 45% identity. DB3S had one intrachain disulfide bond located at Cys 28 -Cys 187 , whereas DB3L had one interchain disulfide bond (Cys 40 -Cys 40 ) in addition to the intrachain disulfide bond (Cys 28 -Cys 188 ) to form a 66-kDa subunit. DB1 and DB3 agglutinated rabbit erythrocytes at 2.7 and 3.9 g/ml, respectively. Despite the structural homology between DB2 and DB3, DB2 had no lectin activity. The 66-kDa subunit itself revealed the full hemagglutinating activity of DB3, indicating that DB3L but not DB3S was responsible for the activity. The hemagglutinating activity of DB3 required Ca 2؉ ions and was exclusively inhibited by maltose and oligomaltoses (e.g. maltopentaose and maltohexaose) but not by D-glucose. DB3 could not be classified into any known plant lectin family. DB4 was a chitinase, homologous to an acidic chitinase from Dioscorea japonica. DB1, DB2, and DB3 did not show any activity of carbonic anhydrase, amylase, or trypsin inhibitor activity. These results show that two of the four major proteins isolated from the yam tubers D. batatas have unique lectin activities.

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Section: Purification and Subunit Structures Of Tubermentioning

confidence: 99%

Characterization of the Yam Tuber Storage Proteins from Dioscorea batatas Exhibiting Unique Lectin Activities

Gaidamashvili¹,

Ohizumi

Iijima

et al. 2004

Journal of Biological Chemistry

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“…In addition to their storage function, they can play additional roles in the plant, e.g. enzymatic (Strickland et al, 1995;Tonón et al, 2001;Rosahl et al, 1987), inhibitory (Yeh et al, 1997;Hou et al, 1999), antioxidant (Hou et al, 2001), antibacterial (Flores et al, 2002) or antifungal ones (Flores et al, 2002, Terras et al, 1993. The storage proteins can be defined as proteins whose major role is to act as stores of nitrogen, sulphur and carbon (Shewry, 2003).…”

Section: Introductionmentioning

confidence: 99%

Protein reutilisation in corms of Colchicum autumnale

et al. 2006

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Colchicum autumnale L. is a monocotyledonous geophyte with hysteranthous leaves, i.e. flowering and leaf growth occur in different time periods. Because after the starch, the second prominent storage compound of corm is represented by proteins, we were interested in nitrogen remobilisation during the annual life cycle of C. autumnale. In this context the content of soluble and insoluble proteins were measured in parallel with determination of some exo-and endopeptidase activities. Our results indicate that the continual proteolysis occurs in both mother and new daughter corms during the whole life-cycle of the plant. L-Ala-aminopeptidase and trypsin-like endopeptidase were the most active peptidases in both mother and daughter corms. As the protein level of mother corm did not change significantly during the development of the future above-ground part under the soil surface (the first, autumnal developmental stage), the developmental profile of nitrate reductase activity was estimated followed by evaluation of total nitrogen and amino acid contents. Significant activity of root nitrate reductase was detected in the roots only in the second, vernal stage. Our results showed that the stored proteins constituted a relevant nitrogen source partly required by the growth processes of the late autumnal stage, but mainly by the intensive growth of leaves and reproductive structures during the second, photosynthetically active stage of the life-cycle.

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“…1). It is well-known that dioscorin, the major tuber storage protein of yam species, accounts for about 90 % of extractable water-soluble proteins in yam species tuber (Hou et al 1999). The dioscorin shows about 32 kDa protein band under reducing condition in SDS-PAGE.…”

Section: Resultsmentioning

confidence: 99%

Functional properties of autolysate and enzymatic hydrolysates from yam tsukuneimo (Dioscorea opposita Thunb.) tuber mucilage tororo: antioxidative activity and antihypertensive activity

Nagai

Suzuki²,

Kai

et al. 2012

J Food Sci Technol

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Yam tsukuneimo tuber mucilage tororo hydrolysates were prepared by autolysis and three different peptic enzymes. Except for pepsin hydrolysate, tororo was perfectly digested. Each hydrolysate for 100 mg/ml significantly prolonged the induction period of auto-oxidation of linoleic acid, which was similar to 5 mM ascorbic acid. These hydrolysates also possessed high scavenging activities such as superoxide anion radicals, hydroxyl radicals, and DPPH radicals. Moreover, high antihypertensive activities were detected in these hydrolysates except for autolysate, which were similar to various fermented foods such as miso, natto, sake, cheese, and so on. Present findings suggest that yam tsukuneimo tuber mucilage tororo may be useful for preventing diseases associated with reactive oxygen species and blood pressure in the body system and it can fully absorb the useful components from it to digest using the gastrointestinal enzymes.

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Dioscorin, the Major Tuber Storage Protein of Yam (Dioscorea batatas Decne) with Carbonic Anhydrase and Trypsin Inhibitor Activities

Cited by 75 publications

References 29 publications

Characterization of the Yam Tuber Storage Proteins from Dioscorea batatas Exhibiting Unique Lectin Activities

Characterization of the Yam Tuber Storage Proteins from Dioscorea batatas Exhibiting Unique Lectin Activities

Protein reutilisation in corms of Colchicum autumnale

Functional properties of autolysate and enzymatic hydrolysates from yam tsukuneimo (Dioscorea opposita Thunb.) tuber mucilage tororo: antioxidative activity and antihypertensive activity

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