PURIFICATION AND CHARACTERIZATION OF MUTANASE PRODUCED BY<i>Paenibacillus curdlanolyticus</i>MP-1

Pleszczyńska, Małgorzata; Wiater, Adrian; Skowronek, Marcin; Szczodrak, Janusz

doi:10.1080/10826068.2011.622329

Cited by 8 publications

(8 citation statements)

References 24 publications

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“…No activity was observed above pH 9.0 (Figure 4A). The results were similar to the bacterial mutanases from P. curdlanolyticus with optimum pH range 5.5-6.5, 25,28 and from S. chartreusis with optimum pH of 5.5-6.0, 27 whereas mutanase from B. circulans was reported to have slightly higher pH range of 7.5-8.5. 14 Most microbial mutanases are stable at the optimum temperature range of 40 • C-59 • C and vary among organisms (Figure 4B).…”

Section: Effect Of Ph and Temperature On Enzyme Activitysupporting

confidence: 77%

“…Average enzyme activity of 0.33 U/mL or 2.5 U/mg was reported in various Trichoderma harzianum strains 22 and 0.82 U/mL or 3.2 U/g of protein in T. harzianum CCM F‐340 when α‐1,3‐glucans were used as a carbon source 23 . Mutanase production from novel isolate C. funkei is comparable with other bacteria such as B. circulans WL‐12 (1.9 U/mg), 14 Paracoccus mutanolyticus (1.18 U/mg), 24 Paenibacillus curdlanolyticus MP‐1 (0.9 U/mg), 25 and Streptomyces sp. KI‐8 strain (0.15 U/mg) 13 .…”

Section: Resultsmentioning

confidence: 94%

“…Similar stimulatory and inhibitory activities using metal ions, protein-modifying agents, and detergents were reported in P. curdlanolyticus, P. mutanolyticus, and S. thermodiastaticus. 24,25,32 However, mutanase enzyme from B. circulans showed no effect with metal ions. glucan from S. pombe) were reported for purified mutanase enzyme from P. curdlanolyticus MP-1.…”

Section: Effect Of Metal Ions and Chemical Agentsmentioning

confidence: 99%

“…The specific activity of the purified enzyme was comparatively higher than other reported purified bacterial mutanases from Bacillus circulans HU-M1 (10 U/mg), 14 and P. curdlanolyticus MP-1 (3.98 U/mg). 25 Purification strategies and biochemical characteristics of various bacterial mutanases are given in Table 3.…”

Section: Purification Of Mutanasementioning

confidence: 99%

“…14 Most microbial mutanases are stable at the optimum temperature range of 40 • C-59 • C and vary among organisms (Figure 4B). Purified mutanases from Trichoderma species were reported with optimum temperature (40 • C-55 • C), 26,29,30 25 B circulans (50 • C), 14 and Pseudomonas sp. (56 • C).…”

Section: Effect Of Ph and Temperature On Enzyme Activitymentioning

confidence: 99%

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Production and application of purified mutanase from novel Cellulosimicrobium funkei SNG1 in the in vitro biofilm degradation

Boddapati

Gummadi

2023

Biotech and App Biochem

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Mutanase (α‐1,3‐glucanase) is an inducible extracellular enzyme with potential medical applications in dentistry. A novel Cellulosimicrobium funkei strain SNG1 producing mutanase enzyme using α‐1,3‐glucans was isolated, and the enzyme was optimized for increased productivity using the one‐factor‐at‐a‐time approach. Maximum growth and enzyme‐specific activity (2.12 ± 0.4 U/mg) were attained in a production medium with pH 7.0 and 1% α‐1,3‐glucans as carbon source, incubated at 37°C for 30 h. The result showed a five‐fold increase in activity compared to unoptimized conditions (0.40 U/mg). The enzyme was purified by gel‐filtration chromatography, and recovered with a yield of 29.03% and a specific activity increase of 10.9‐fold. The molecular mass of the monomeric enzyme is 137 kDa. The pH and temperature optima are 6.0 and 45°C with Km of 1.28 ± 0.11 mg for α‐1,3‐glucans. The enzyme activity was stimulated by adding Co2+, Ca2+, Cu2+, and was entirely inhibited by Hg2+. On 2‐h incubation, the purified enzyme effectively degraded in vitro film with an 82.68% degradation rate and a saccharification yield of 30%.

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