Studies on pH and thermal deactivation of pectolytic enzymes from Aspergillus niger

Naidu, G. S. N.; Panda, T.

doi:10.1016/s1369-703x(03)00022-6

Cited by 89 publications

(46 citation statements)

References 26 publications

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“…On the other hand, after the same time of treatment at 25, 30 and 40ºC, almost all enzyme activity was preserved. The total inactivation of endo-PG was quickly noticed after about 15 minutes at 60 and 70ºC, as reported by Naidu and Panda (2003) for polygalacturonase produced by A. niger in submerged process. This study corroborated the conclusions reported by Daniel (1996), who suggested the low stability of enzymes at temperatures higher than the ideal for the microbial growth.…”

Section: Resultssupporting

confidence: 75%

Production and characterization of endo-polygalacturonase from Aspergillus niger in solid-state fermentation in double-surface bioreactor

Hendges

Montanari

Malvessi

et al. 2011

Braz. arch. biol. technol.

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Section: Resultssupporting

confidence: 75%

Production and characterization of endo-polygalacturonase from Aspergillus niger in solid-state fermentation in double-surface bioreactor

Hendges

Montanari

Malvessi

et al. 2011

Braz. arch. biol. technol.

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“…Several studies on microbial enzymes have shown the production of multiple pectinase forms which differ on molecular mass and kinetic properties [15,46,47]. The production of multiple forms of enzymes improves the microorganism ability to adapt to environmental modifications [48].…”

Section: Microbial Pectinasesmentioning

confidence: 99%

Pectin and Pectinases: Production, Characterization and Industrial Application of Microbial Pectinolytic Enzymes

Pedrolli¹,

Monteiro²,

Gomes³

et al. 2009

TOBIOTJ

280

123

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Pectinases are a big group of enzymes that break down pectic polysaccharides of plant tissues into simpler molecules like galacturonic acids. It has long been used to increase yields and clarity of fruit juices. Since pectic substances are a very complex macromolecule group, various pectinolytic enzymes are required to degrade it completely. These enzymes present differences in their cleavage mode and specificity being basically classified into two main groups that act on pectin "smooth" regions or on pectin "hairy" regions. Pectinases are one of the most widely distributed enzymes in bacteria, fungi and plants. This review describes the pectinolytic enzymes and their substrates, the microbial pectinase production and characterization, and the industrial application of these enzymes.

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“…Inactivation is defined as a process where the secondary, tertiary or quaternary structure of a protein changes without breaking covalent bonds. The inactivation of pectolytic enzymes is assumed to follow first order kinetics [29]. Inactivation rate constants (k d ) of exo-polygalacturonase which are presented in Table 2 (at 75, 80, 82.5 and 85 • C) were calculated from the slope of semilogarithmic plot of residual activity versus time.…”

Section: Kinetics Of Thermal Inactivation and Estimation Of The Inactmentioning

confidence: 99%

Characterization of three-phase partitioned exo-polygalacturonase from Aspergillus sojae with unique properties

Dogan¹,

Tarı²

2008

Biochemical Engineering Journal

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Exo-polygalacturonase enzyme produced by Aspergillus sojae ATCC 20235 was purified using three-phase partitioning (TPP), an emerging bio-separation technique where a single step as compared to the classical multi-step purification was used. Using this technique, crude enzyme solution (pH 6.6) saturated to 30% (w/v) with ammonium sulphate and with a crude extract to tert-butanol ratio of 1:1 (v/v) at 25• C resulted in 25.5% recovery of exo-polygalacturonase with a 6.7-fold purification. The purified enzyme was characterized with respect to its activity and stability at various pH and temperature ranges. Optimum pH and temperature for maximum activity were determined as pH 4 and 55• C. The enzyme was stable at both acidic and alkaline pH for 2 h at 30• C. The thermal stability study showed that the purified enzyme had an inactivation energy of 68.41 kcal/mol and a half-life (t 1/2 ) value of 3.6 h at 75• C presenting a large thermal stability. The kinetic constants K m and V max using polygalacturonic acid as substrate were 0.75 g l −1 and 1.14 mol min −1 , respectively. SDS-PAGE profiling revealed that the purified exopolygalacturonase had two bands with the molecular weights of 36 and 53 kDa. The enzyme was completely inhibited in the presence of Mn 2+ and SDS and induced significantly by EDTA, glycerol and ␤-mercaptoethanol.

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Studies on pH and thermal deactivation of pectolytic enzymes from Aspergillus niger

Cited by 89 publications

References 26 publications

Production and characterization of endo-polygalacturonase from Aspergillus niger in solid-state fermentation in double-surface bioreactor

Production and characterization of endo-polygalacturonase from Aspergillus niger in solid-state fermentation in double-surface bioreactor

Pectin and Pectinases: Production, Characterization and Industrial Application of Microbial Pectinolytic Enzymes

Characterization of three-phase partitioned exo-polygalacturonase from Aspergillus sojae with unique properties

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