Papaya β-galactosidase/galactanase isoforms in differential cell wall hydrolysis and fruit softening during ripening

Lazan, Hamid; Ng, S P; Goh, Lee-Yin; Ali, Zuraidah

doi:10.1016/j.plaphy.2004.10.007

Cited by 77 publications

(53 citation statements)

References 30 publications

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“…In plants, they are associated with secondary metabolism or polysaccharide degradation, performing important roles in physiological events, including cell wall degradation and expansion during plant development, and turnover of signaling molecules [79][80][81][82][83]. They were also shown to be involved in ripening and abscission of mango, papaya, and orange fruits [84][85][86]. The GH35 found in the cell wall proteomes of sugarcane [30] and B. distachyon [31] is predicted to have a β-galactosidase activity (GO:0004565).…”

Section: Gh27 and Gh35mentioning

confidence: 99%

Glycoside Hydrolases in Plant Cell Wall Proteomes: Predicting Functions That Could Be Relevant for Improving Biomass Transformation Processes

Calderan-Rodrigues¹,

Fonseca²,

Clemente³

et al. 2018

Advances in Biofuels and Bioenergy

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Glycoside hydrolases (GHs) are enzymes that are able to rearrange the plant cell wall polysaccharides, being developmental-and stress-regulated. Such proteins are used in enzymatic cocktails for biomass hydrolysis in the second-generation ethanol (E2G) production. In this chapter, we investigate GHs identified in plant cell wall proteomes by predicting their functions through alignment with homologous plant and microorganism sequences and identification of functional domains. Up to now, 49 cell wall GHs were identified in sugarcane and 114 in Brachypodium distachyon. We could point at candidate proteins that could be targeted to lower biomass recalcitrance. We more specifically addressed several GHs with predicted cellulase, hemicellulase, and pectinase activities, such as β-xylosidase, α and β-galactosidase, α-N-arabinofuranosidases, and glucan β-glucosidases. These enzymes are among the most used in enzymatic cocktails to deconstruct plant cell walls. As an example, the fungi arabinofuranosidases belonging to the GH51 family, which were also identified in sugarcane and B. distachyon, have already been associated to the degradation of hemicellulosic and pectic polysaccharides, through a peculiar mechanism, probably more efficient than other GH families. Future research will benefit from the information available here to design plant varieties with self-disassembly capacity, making the E2G more cost-effective through the use of more efficient enzymes.

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Section: Gh27 and Gh35mentioning

confidence: 99%

Glycoside Hydrolases in Plant Cell Wall Proteomes: Predicting Functions That Could Be Relevant for Improving Biomass Transformation Processes

Calderan-Rodrigues¹,

Fonseca²,

Clemente³

et al. 2018

Advances in Biofuels and Bioenergy

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“…Although the mechanisms by which b-galactosidases are involved in cell wall modifications are not entirely clear, a functional role for b-galactosidases that alter wall properties during fruit ripening has been demonstrated. For example, the carambola b-galactosidase from ripe fruit is active against various galactans and can depolymerize structurally intact pectin and modify hemicelluloses (Balasubramaniam et al, 2005), and papaya b-galactosidase from ripe fruit has been shown to be capable of hydrolyzing cell wall components in unripe fruit (Lazan et al, 2004). It may be that there are analogies between fruit ripening and mucilage modification in the seed coat.…”

Section: The Impacts Of Pectin Modification On Cell Wall Propertiesmentioning

confidence: 99%

The Arabidopsis MUM2 Gene Encodes a β-Galactosidase Required for the Production of Seed Coat Mucilage with Correct Hydration Properties

et al. 2007

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Seed coat development in Arabidopsis thaliana involves a complex pathway where cells of the outer integument differentiate into a highly specialized cell type after fertilization. One aspect of this developmental process involves the secretion of a large amount of pectinaceous mucilage into the apoplast. When the mature seed coat is exposed to water, this mucilage expands to break the primary cell wall and encapsulate the seed. The mucilage-modified2 (mum2) mutant is characterized by a failure to extrude mucilage on hydration, although mucilage is produced as normal during development. The defect in mum2 appears to reside in the mucilage itself, as mucilage fails to expand even when the barrier of the primary cell wall is removed. We have cloned the MUM2 gene and expressed recombinant MUM2 protein, which has b-galactosidase activity. Biochemical analysis of the mum2 mucilage reveals alterations in pectins that are consistent with a defect in b-galactosidase activity, and we have demonstrated that MUM2 is localized to the cell wall. We propose that MUM2 is involved in modifying mucilage to allow it to expand upon hydration, establishing a link between the galactosyl side-chain structure of pectin and its physical properties.

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“…The loss of activity of the enzyme at higher temperatures could be attributed to its unfolding and subsequent loss of active site [17]. The optimum temperature of β-galactosidase was in the range 40-60°C [27,28,30]. …”

Section: Optimum Temperaturementioning

confidence: 99%

Extraction, Purification and Characterization of Apricot Seed β-Galactosidase for Producing Free Lactose Cheese

Yossef¹

2014

J Nutr Food Sci

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Abstractβ-Galactosidase was extracted (with acetate buffer pH 5) from apricot seeds, partially purified by ammonium sulphate (30-70%) and dialyzed for 24 hr. The crude extract had a higher specific activity (9.93 U/mg proteins) which indicates a high enzyme yield. Purification of crude extract with ammonium sulphate (30-70%) increased the specific activity and purification fold to 29.07 U/mg proteins and 2.92, respectively which was improved by dialysis to 32.68 U/mg proteins and 3.29, respectively. The extracted enzyme exhibits an optimum temperature at 70°C and 5 pH optima. The enzyme activity was almost stable between pH 5.0 and 6.5, where more than 90% of its activity was remained with incubation at the previous pH for 30 min. Further more; it was thermostable when incubated for 30 min. at temperature ranges of 55-70°C with a complete loss of activity at 80°C. The activity of β-galactosidase was enhanced by different concentration of Ca +2 . There were no significant (P>0.05) changes in flavor, body texture, and overall acceptability between free lactose white cheese treated by apricot seeds β -galactosidase (9865 U/ 500 ml milk) and untreated cheese.

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Papaya β-galactosidase/galactanase isoforms in differential cell wall hydrolysis and fruit softening during ripening

Cited by 77 publications

References 30 publications

Glycoside Hydrolases in Plant Cell Wall Proteomes: Predicting Functions That Could Be Relevant for Improving Biomass Transformation Processes

Glycoside Hydrolases in Plant Cell Wall Proteomes: Predicting Functions That Could Be Relevant for Improving Biomass Transformation Processes

The Arabidopsis MUM2 Gene Encodes a β-Galactosidase Required for the Production of Seed Coat Mucilage with Correct Hydration Properties

Extraction, Purification and Characterization of Apricot Seed β-Galactosidase for Producing Free Lactose Cheese

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