Purification and enzymatic properties of α‐galactosidase from <i>Penicillium janthinellum</i>

Elshafei, Ali M.; Foda, M. S.; Aboul‐Enein, Ahmed M.; Afify, A. M.; Ali, Nadia H.

doi:10.1002/abio.370130407

Cited by 3 publications

(3 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…AGLIII (61 kDa) were rather similar to those of α-galactosidases purified from other Penicillium species [4,5,38,39]. However, their isoelectric points were more basic (AGLI, 5.2 ; AGLIII, 7) compared with 4.0-4.3 of other Penicillium αgalactosidases studied.…”

Section: Discussionmentioning

confidence: 71%

“…P. simplicissimum AGLII differed completely from the other two α-galactosidases produced, as it was larger. Thus AGLII resembled more the bacterial, yeast or Aspergillus αgalactosidases than the other Penicillium enzymes [21,38,39,[43][44][45][46]. Furthermore, AGLII possessed significantly higher specific activity on the basis of the pNPG assay than AGLI and AGLIII, and was more resistant towards endproduct inhibition.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

α‐Galactosidases of Penicillium simplicissimum: production, purification and characterization of the gene encoding AGLI

Luonteri,

Alatalo,

Siika‐aho

et al. 1998

Biotech and App Biochem

View full text Add to dashboard Cite

Production of extracellular a‐galactosidases by the filamentous fungus Penicillium simplicissimum (previously P. janthinellum) VTT‐D‐78090 was studied on different carbon sources. Steam‐exploded oat husks were chosen as the best carbon source for enzyme production. Three a‐galactosidases (AGL) were purified from the culture filtrate using ion‐exchange chromatography, hydrophobic interaction chromatography and gel filtration. The isoelectric points of AGLI, AGLII and AGLIII were 5.2, 4.4 and 7.0, and the molecular masses as determined by SDS/PAGE were 61, 84 and 61 kDa, respectively. All enzymes were glycosylated. The optimum pH for the activity of AGLI and AGLIII was between 3.0 and 4.5 and that of AGLII was between 4.0 and 5.0. AGLII was more stable and more resistant to product inhibition by galactose than the other two enzymes. AGLI and AGLIII were also inhibited by p‐nitrophenol‐a‐D‐galactopyranoside, the substrate used for enzyme activity assay. The gene encoding AGLI was cloned and sequenced. The gene, agl1, encodes 435 amino acids including the signal sequence. It showed similarity with the other a‐galactosidases belonging to the glycosyl hydrolase family 27. The N‐terminal amino acid sequence of AGLIII was also similar to the sequences of other members of family 27, whereas the N‐terminus of AGLII was completely different from the sequences of other reported hydrolases.

show abstract

Section: Discussionmentioning

confidence: 71%

Section: Discussionmentioning

confidence: 99%

α‐Galactosidases of Penicillium simplicissimum: production, purification and characterization of the gene encoding AGLI

Luonteri,

Alatalo,

Siika‐aho

et al. 1998

Biotech and App Biochem

View full text Add to dashboard Cite

show abstract

“…Various microorganisms such as fungus [11, 13], yeasts [14], and bacteria [15] produce α -galactosidase. It has been documented that several α -galactosidases could be translated by Penicillium ochrochloron, P. purpurogenum [16], P. simplicissimum [17], and P. brevicompactum [18]. In addition, abundant information is available on the biosynthesis of α -galactosidase from filamentous fungi belonging to the different genera of Aspergillus [19–21].…”

Section: Introductionmentioning

confidence: 99%

Optimization of Culture Conditions for Some Identified Fungal Species and Stability Profile ofα-Galactosidase Produced

Chauhan

Srivastava

Kehri

et al. 2013

Biotechnology Research International

View full text Add to dashboard Cite

Microbial α-galactosidase preparations have implications in medicine and in the modification of various agricultural products as well. In this paper, four isolated fungal strains such as AL-3, WF-3, WP-4 and CL-4 from rhizospheric soil identified as Penicillium glabrum (AL-3), Trichoderma evansii (WF-3), Lasiodiplodia theobromae (WP-4) and Penicillium flavus (CL-4) based on their morphology and microscopic examinations, are screened for their potential towards α-galactosidases production. The culture conditions have been optimized and supplemented with specific carbon substrates (1%, w/v) by using galactose-containing polysaccharides like guar gum (GG), soya casein (SC) and wheat straw (WS). All strains significantly released galactose from GG, showing maximum production of enzyme at 7th day of incubation in rotary shaker (120 rpm) that is 190.3, 174.5, 93.9 and 28.8 U/mL, respectively, followed by SC and WS. The enzyme activity was stable up to 7days at −20°C, then after it declines. This investigation reveals that AL-3 show optimum enzyme activity in guar gum media, whereas WF-3 exhibited greater enzyme stability. Results indicated that the secretion of proteins, enzyme and the stability of enzyme activity varied not only from one strain to another but also differed in their preferences of utilization of different substrates.

show abstract

α-Galactosidases

Anisha¹

2017

Current Developments in Biotechnology and Bioengineering

View full text Add to dashboard Cite

Purification and enzymatic properties of α‐galactosidase from Penicillium janthinellum

Cited by 3 publications

References 12 publications

α‐Galactosidases of Penicillium simplicissimum: production, purification and characterization of the gene encoding AGLI

α‐Galactosidases of Penicillium simplicissimum: production, purification and characterization of the gene encoding AGLI

Optimization of Culture Conditions for Some Identified Fungal Species and Stability Profile ofα-Galactosidase Produced

α-Galactosidases

Contact Info

Product

Resources

About