Characterisation of a β-N-acetylhexosaminidase from a commercial papaya latex preparation

Chen, Lichun; Chung, Yun‐Chin; Chang, Ya-Min; Chang, Chi-Wei

doi:10.1016/j.foodchem.2010.07.099

Cited by 8 publications

(7 citation statements)

References 30 publications

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“…The isoelectric point of the enzyme was determined by IFGE. The result shows that the pI value of the enzyme was approximately 5.54, which is close to that of porcine semen acidic NAGase (Huang et al, 2009), and same as papaya NAGase (Chen et al, 2011). However, this value was different from that of the Bombyx mori alimentary canal (pI 4.86) (Koga et al, 1986) and Penaeus vannamei (pI 4.8) NAGases.…”

Section: Determination Of the Isoelectric Point Of The Enzymementioning

confidence: 58%

“…Crustacean NAGase is related to chitin metabolism, and it participates in the molting process (Xie et al, 2004). NAGase in plants is related to glycan metabolism and defense functions (Chen et al, 2011). NAGase in mammals is mainly related to the synthesis and degradation of glycan in glycoproteins and is involved in the physiological process of sperm and egg binding (Miller et al, 1993;Shur and Hall, 1982).…”

Section: Discussionmentioning

confidence: 99%

“…The optimal temperature of hetian chicken testicle NAGase is 55°C, and it is stable at 10 to 60°C (Jin et al, 2009). The optimal temperature of papaya NAGase is 50°C, and it is stable at 30 to 45°C; however, its enzyme activity rapidly decreases at temperatures higher than 50°C (Chen et al, 2011). 1or in 0.15 M Na 2 HPO 4 -NaH 2 PO 4 buffer (2), the concentration of substrate was 0.5 mM.…”

Section: Effects Of Temperature On the Enzyme Activity And Thermal Stmentioning

confidence: 99%

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Purification and properties of N-acetyl--D glucosaminidase from bovine testicle

Huang¹,

Jin²,

Huang³

et al. 2013

Afr. J. Biotechnol.

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N-Acetyl-β-D-glucosaminidase (NAGase) from bovine testicle was purified by ammonium sulfate fractionation followed by diethylaminoethyl (DEAE)-cellulose (DEAE-32) and Sephacryl S-300 chromatography. The enzyme was purified to homogeneity as analyzed by polyacrylamide gel electrophoresis (PAGE) and isoelectric focusing gel electrophoresis (IFGE). The specific activity of the purified enzyme was 658.21 U/mg. The enzyme was a single subunit with molecular weight of 68.3 kDa and contained 3.03% sugar. The pI value was calculated to be 5.54 using IFGE. The optimal pH and temperature of the enzyme for hydrolysis of p-Nitrophenyl-N-acetyl-β-D-glucosaminide (pNP-NAG) were found to be pH 5.6 and 50°C, respectively. The kinetics results showed that the enzyme hydrolyzed pNP-NAG following Michaelis-Menten with K m of 0.71 mM and V m of 16.72 M/min at pH 5.6 and 37°C. The enzyme was stable at pH values ranging from 2 to 6.5 and at temperatures below 60°C. The activation energy was determined to be 64.19 kJ/mol.

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Section: Determination Of the Isoelectric Point Of The Enzymementioning

confidence: 58%

Section: Discussionmentioning

confidence: 99%

Section: Effects Of Temperature On the Enzyme Activity And Thermal Stmentioning

confidence: 99%

See 1 more Smart Citation

Purification and properties of N-acetyl--D glucosaminidase from bovine testicle

Huang¹,

Jin²,

Huang³

et al. 2013

Afr. J. Biotechnol.

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“…Corroborating the results obtained from the characterization of the novel enzyme and its optimal activity (30 °C; pH 5.0; 0.5 M; 3h/stability), Ogawa et al [ 55 ] described similar temperature and pH optimal conditions (37 °C and pH 5.5). The pH values ranging from 4.0 to 6.0 are known to be typical for the substrates tested here [ 56 , 57 ]. The optimal temperature for enzymatic activity is modulated according to the environmental conditions [ 58 , 59 ].…”

Section: Discussionmentioning

confidence: 99%

A Novel Multifunctional β-N-Acetylhexosaminidase Revealed through Metagenomics of an Oil-Spilled Mangrove

et al. 2017

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The use of culture-independent approaches, such as metagenomics, provides complementary access to environmental microbial diversity. Mangrove environments represent a highly complex system with plenty of opportunities for finding singular functions. In this study we performed a functional screening of fosmid libraries obtained from an oil contaminated mangrove site, with the purpose of identifying clones expressing hydrolytic activities. A novel gene coding for a β-N-acetylhexosaminidase with 355 amino acids and 43KDa was retrieved and characterized. The translated sequence showed only 38% similarity to a β-N-acetylhexosaminidase gene in the genome of Veillonella sp. CAG:933, suggesting that it might constitute a novel enzyme. The enzyme was expressed, purified, and characterized for its enzymatic activity on carboxymethyl cellulose, p-Nitrophenyl-2acetamide-2deoxy-β-d-glucopyranoside, p-Nitrophenyl-2acetamide-2deoxy-β-d-galactopyranoside, and 4-Nitrophenyl β-d-glucopyranoside, presenting β-N-acetylglucosaminidase, β-glucosidase, and β-1,4-endoglucanase activities. The enzyme showed optimum activity at 30 °C and pH 5.5. The characterization of the putative novel β-N-acetylglucosaminidase enzyme reflects similarities to characteristics of the environment explored, which differs from milder conditions environments. This work exemplifies the application of cultivation-independent molecular techniques to the mangrove microbiome for obtaining a novel biotechnological product.

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“…Firstly, β-N-acetylhexosaminidase participates in physiological processes such as seed germination and fruit ripening. In dry or germinating seeds β-N-acetylhexosaminidase is highly active and is considered to function in the degradation of reserve glycoproteins [10,11]. In tomato, capsicum and peach fruits β-Nacetylhexosaminidase and α-mannosidase activity is presumed to play a role in ripening and softening of fruits by releasing of free N-glycans affecting ethylene biosynthesis [12][13][14][15].…”

mentioning

confidence: 99%

Different Roles of ÃÂ²-N-Acetylhexosaminidase in Metabolism

Hýsková¹

2015

Biochem Anal Biochem

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typically found in plants and invertebrate [16]. These structures are characterized by the presence of fucose and/or xylose, which can be transferred to the oligosaccharide core only after removal of the terminal GlcNAc (catalyzed by β-N-acetylhexosaminidase) from the complex oligosaccharide. It is interesting that this step of N-glycan processing occurs in plants in vacuole rather than Golgi apparatus.

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Characterisation of a β-N-acetylhexosaminidase from a commercial papaya latex preparation

Cited by 8 publications

References 30 publications

Purification and properties of N-acetyl--D glucosaminidase from bovine testicle

Purification and properties of N-acetyl--D glucosaminidase from bovine testicle

A Novel Multifunctional β-N-Acetylhexosaminidase Revealed through Metagenomics of an Oil-Spilled Mangrove

Different Roles of ÃÂ²-N-Acetylhexosaminidase in Metabolism

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Characterisation of a β-N-acetylhexosaminidase from a commercial papaya latex preparation

Cited by 8 publications

References 30 publications

Purification and properties of N-acetyl--D glucosaminidase from bovine testicle

Purification and properties of N-acetyl--D glucosaminidase from bovine testicle

A Novel Multifunctional β-N-Acetylhexosaminidase Revealed through Metagenomics of an Oil-Spilled Mangrove

Different Roles of ÃÂ²-N-Acetylhexosaminidase in Metabolism

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Different Roles of ÃÂ²-N-Acetylhexosaminidase in Metabolism