Glycosidases of apple fruit: A multi-functional beta-galactosidase

Dick, Arthur J.; Opoku-Gyamfua, Angelina; DeMarco, Alphonse C.

doi:10.1034/j.1399-3054.1990.800214.x

Cited by 7 publications

(7 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…At 59 kDa, the size of the active enzyme is very similar to 13-galactosidases from other tissues (Pressey 1983;Dopico et al 1989;Sekimata et al 1989;Simos et al 1989;Burns 1990;Dick et al 1990;Giannakouros et al 1991). However, the size is at variance with a 145-kDa kiwifruit [3-galactosidase purified previously (Ogawa et al 1990).…”

Section: Discussionmentioning

confidence: 92%

“…Others have also reported difficulty in maintaining active, purified 13-galactosidase in storage (Burns 1990;Dick et al 1990;Kundu et al 1990), and have observed the continued appearance of low-molecular-weight bands in SDS-PAGE of purified 13-galactosidase (Edwards et al 1988). With our kiwifruit enzyme preparation, the predominant band on an acidic non-denaturing gel was associated with enzyme activity (Fig.…”

Section: Discussionmentioning

confidence: 93%

“…Bartley 1974;Pressey 1983;Wegrzyn and MacRae 1992). Some degree of purification and characterisation of 13-galactosidase has been reported from a number of fruit, including tomato (Pressey 1983), apple (Dick et al 1990), orange (Burns 1990) and kiwifruit (Ogawa et al 1990). In tomato, increased amounts of galactose derived from cell-wall polysaccharides during fruit ripening were found to be due to changes in the rate of galactosyl solubilisation from the wall rather than changes in metabolic utilisation of the solubilised galactose (Kim et al 1991).…”

Section: Introductionmentioning

confidence: 98%

See 2 more Smart Citations

Kiwifruit ?-galactosidase: Isolation and activity against specific fruit cell-wall polysaccharides

Ross

Redgwell

MacRae

1993

Planta

129

View full text Add to dashboard Cite

Abstract.A [3-galactosidase (EC 3.2.1.23) capable of degrading a number of fruit cell-wall polysaccharides in vitro, was isolated from ripening kiwifruit (Actinidia deliciosa [A. Chev.] C.F. Liang et A.R. Ferguson cv. Hayward). The enzyme has a molecular weight of approximately 60 kDa by gel permeation and consists of several basic isoforms. Several polypeptides were enriched during purification, with 33-, 46-and 67-kDa bands being predominant after sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The optimum activity of the enzyme against p-nitrophenyl-[3-D-galactopyranoside was at pH 3.2, but against a galactan purified from kiwifruit cell walls, it was at pH 4.9. The enzyme was specific for galactosyl residues in the [3-configuration, releasing galactose from a variety of kiwifruit cell-wall polysaccharide fractions including cell wall material, Na2CO3-soluble pectin, high-molecular-weight galactan, xyloglucan, and galactoglucomannan. A galactosylated glucuronomannan found throughout the kiwifruit plant was also a substrate for the enzyme. The results indicate that the enzyme attacks the non-reducing end of galactose side chains, cleaving single galactose residues which may be attached to the 2, 3, 4, or 6 position of the aglycone. Activity of the enzyme in-vitro was too low to account for the total loss of galactose from the cell walls during ripening. If the [3-galactosidase of this study is solely responsible for the removal of galactose from the cell wall during ripening then its in-vivo activity must be much greater than that observed in-vitro.

show abstract

Section: Discussionmentioning

confidence: 92%

Section: Discussionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 98%

See 1 more Smart Citation

Kiwifruit ?-galactosidase: Isolation and activity against specific fruit cell-wall polysaccharides

Ross

Redgwell

MacRae

1993

Planta

129

View full text Add to dashboard Cite

show abstract

“…Yoshioka et al (1992) suggested that Percy et al (1996) Abeles& Biles (1991) *In vivo substrates and sites of action are yet to be confirmed, as there is some suggestion that P-galactosidase may also have associated a-L-arabinopyranosidase and P-D-fucosidase activities (Dick et al 1990). '''This is isozyme dependent, as one isozyme increased, while three isozymes decreased, during ripening in apples (Yoshioka et al 1995).…”

Section: Cell Wallmentioning

confidence: 99%

Postharvest softening of apple (Malus domestica) fruit: A review

Johnston

Hewett²,

Hertog

2002

New Zealand Journal of Crop and Horticultural Science

207

136

View full text Add to dashboard Cite

Postharvest softening of apple (Malus domestica (Borkh.)) fruit is a serious problem for growers in many countries, including New Zealand. To reduce this problem considerable research has been undertaken to determine the biological causes of softening so that this process can be managed or controlled more effectively. This review describes the pattern of softening for harvested apple fruit, and how it is influenced by different preharvest, atharvest, and postharvest factors. Information is also given on the likely physiological and biochemical causes of apple softening, such as fruit anatomy and cell packing, modification of the cell wall and membranes, changes in cell turgor, and the role of ethylene and other growth regulators. Despite many softening studies, there is still a poor understanding of what causes firmness variation in the marketplace. Until this understanding is improved, apple producers will continue to struggle to meet market requirements for texture.

show abstract

“…The enzyme has been implicated in a number of biological processes, including plant growth and fruit ripening. Softening-related βgals have been purified from the fruits of tomato (Pressy, 1983;Carey et al, 1995;Carrington and Pressy, 1996), apple (Knee, 1973;Dick et al, 1990;Ross et al, 1994;Yoshioka et al, 1994), muskmelon (Cucumis melo) (Ranwala et al, 1992), avocado (Persea americana) (De Veau et al, 1993), kiwifruit (Ross et al, 1993), coffee (Coffea arabica) (Golden et al, 1993), persimmon (Diospyros kaki) (Kang et al, 1994), mango (Mangifeera indica) (Ali et al, 1995), and Japanese pear (Kitagawa et al, 1995) plants and their biochemical properties have been identified.…”

Section: Introductionmentioning

confidence: 99%

Comprehensive analysis of beta-galactosidase protein in plants based on Arabidopsis thaliana

Seddigh¹,

Darabi²

2014

Turk J Biol

View full text Add to dashboard Cite

Beta-galactosidases (βgals) (EC 3.2.1.23) have been detected in a wide range of plant organs and tissues and are described by their ability to hydrolyze terminal nonreducing β-D-galactosyl residues from β-D-galactosides. In this study, 92 βgal protein sequences from different plants, 7 animal samples including human and mouse, 3 samples from bacteria including Escherichia coli, and 4 samples from insects including Drosophila melanogaster were aligned. Sequences were analyzed by computational tools to predict the protein properties, such as molecular mass, isoelectric point, signal peptide, motifs, transmembrane domain, and secondary and spatial structure. Protein structure analysis revealed there is a high identity between plants and other organisms. The modeled βgal has a typical spatial structure with catalytic regions. The 3-dimensional model of Arabidopsis thaliana βgal (Accession Number: NP_001154292) was further checked by PROCHECK algorithm, and showed the majority of the amino acid residues were located in the most-favored regions in a Ramachandran plot. This result suggested that the simulated 3-dimensional structure was reliable. Phylogenetic analysis indicated that A. thaliana βgal has a close relationship with some plants' βgal from different families such as Malvaceae, Solanaceae, and Poaceae. According to these results, βgals should be derived from a common ancestor.

show abstract

Glycosidases of apple fruit: A multi-functional beta-galactosidase

Cited by 7 publications

References 0 publications

Kiwifruit ?-galactosidase: Isolation and activity against specific fruit cell-wall polysaccharides

Kiwifruit ?-galactosidase: Isolation and activity against specific fruit cell-wall polysaccharides

Postharvest softening of apple (Malus domestica) fruit: A review

Comprehensive analysis of beta-galactosidase protein in plants based on Arabidopsis thaliana

Contact Info

Product

Resources

About