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  1. Lee KC, Tong WY, Ibrahim D, Arai T, Murata Y, Mori Y, et al.
    Appl Biochem Biotechnol, 2017 Jan;181(1):451-463.
    PMID: 27596245 DOI: 10.1007/s12010-016-2223-4
    Application of microbial enzymes for paper deinking is getting tremendous attention due to the rapidly increasing of waste paper every year. This study reports the deinking efficiency of laser-printed paper by the lignocellulolytic enzyme from Penicillium rolfsii c3-2(1) IBRL strain compared to other enzyme sources as well as commercial available enzymes. High enzymatic deinking efficiency of approximately 82 % on laser-printed paper was obtained by pulp treatment with crude enzyme from P. rolfsii c3-2(1) IBRL. However, this crude enzyme was found to reduce the paper strength properties of the pulp based on the results of tensile, tear and burst indices, most probably due to the cellulose degradation. This was further proven by the low viscosity of paper pulp obtained after enzymatic treatment and increasing of sugar production during the treatment. Balancing to this detrimental effect on paper pulp, high deinking efficiency was achieved within a short period of time, in which the enzymatic treatment was conducted for 30 min that enabled contribution to higher brightness index obtained, thus promoting savings of time and energy consumption, therefore environmental sustainability. Extensive research should be conducted to understand the nature and mechanism of enzymatic deinking process by the crude enzyme from P. rolfsii c3-2(1) IBRL in order to improve paper strength properties.
    Matched MeSH terms: Penicillium/enzymology*
  2. Alam MZ, Fakhru'l-Razi A, Molla AH
    Water Res, 2003 Sep;37(15):3569-78.
    PMID: 12867323
    The biosolids accumulation and biodegradation of domestic wastewater treatment plant (DWTP) sludge by filamentous fungi have been investigated in a batch fermenter. The filamentous fungi Aspergillus niger and Penicillium corylophilum isolated from wastewater and DWTP sludge was used to evaluate the treatment performance. The optimized mixed inoculum (A. niger and P. corylophilum) and developed process conditions (co-substrate and its concentration, temperature, initial pH, inoculum size, and aeration and agitation rate) were incorporated to accelerate the DWTP sludge treatment process. The results showed that microbial treatment of higher strength of DWTP sludge (4% w/w of TSS) was highly influenced by the liquid state bioconversion (LSB) process. In developed bioconversion processes, 93.8 g/kg of biosolids was enriched with fungal biomass protein of 30 g/kg. Enrichment of nutrients such as nitrogen (N), phosphorous (P), potassium (K) in biosolids was recorded in 6.2% (w/w), 3.1% (w/w) and 0.15% (w/w) from its initial values of 4.8% (w/w), 2.0% (w/w) and 0.08% (w/w) respectively after 10 days of fungal treatment. The biodegradation results revealed that 98.8% of TSS, 98.2% of TDS, 97.3% of turbidity, 80.2% of soluble protein, 98.8% of reducing sugar and 92.7% of COD in treated DWTP sludge supernatant were removed after 8 days of microbial treatment. The specific resistance to filtration (SRF) in treated sludge (1.4x10(12) m/kg) was decreased tremendously by the microbial treatment of DWTP sludge after 6 days of fermentation compared to untreated sample (85x10(12) m/kg).
    Matched MeSH terms: Penicillium/enzymology*
  3. Alhelli AM, Abdul Manap MY, Mohammed AS, Mirhosseini H, Suliman E, Shad Z, et al.
    PMID: 27836491 DOI: 10.1016/j.jchromb.2016.10.037
    This report shows the partitioning and purification of alkaline extracellular lipase from Penicillium candidum (PCA 1/TT031) by solid-state fermentation (SSF). In the present analysis, some of the important parameters such as PEG concentration, PEG molecular mass, salt concentration and buffer concentration were optimised through the response surface methodology (RSM). The optimum aqueous two-phase systems (ATPS) environment consisted of 13.8% (w/w) phosphate buffer, 9.2% (w/w) PEG-3000 and 3.3% (w/w) NaCl at 25°C. The RSM approach was proved to be the most suitable methodology for the recovery of desired enzymes. In this method, the enzyme partitioned into the top phase of the PEG-buffer-NaCl ATPS. Under this experimental environment, the purification factor was found to be 33.9, the partition coefficient was 4.0 and the yield was found to be 84.0% of lipase. Moreover, the experimental and predicted results were in considerable agreement, which established the reliability and validity of the proposed model. The ATPS methodology is proven to be effective for the primary recovery of lipase at a low cost with a large loading capacity and possibility of linear scale up. In addition to using the existing methodologies for improving enzyme production, the use of statistical optimisation of the constituents of phases through RSM continues to be the basic and practical method.
    Matched MeSH terms: Penicillium/enzymology*
  4. Alhelli AM, Abdul Manap MY, Mohammed AS, Mirhosseini H, Suliman E, Shad Z, et al.
    Int J Mol Sci, 2016 Nov 11;17(11).
    PMID: 27845736
    Penicillium candidum (PCA 1/TT031) synthesizes different types of extracellular proteases. The objective of this study is to optimize polyethylene glycol (PEG)/citrate based on an aqueous two-phase system (ATPS) and Response Surface Methodology (RSM) to purify protease from Penicillium candidum (PCA 1/TT031). The effects of different PEG molecular weights (1500-10,000 g/mol), PEG concentration (9%-20%), concentrations of NaCl (0%-10%) and the citrate buffer (8%-16%) on protease were also studied. The best protease purification could be achieved under the conditions of 9.0% (w/w) PEG 8000, 5.2% NaCl, and 15.9% sodium citrate concentration, which resulted in a one-sided protease partitioning for the bottom phase with a partition coefficient of 0.2, a 6.8-fold protease purification factor, and a yield of 93%. The response surface models displayed a significant (p ≤ 0.05) response which was fit for the variables that were studied as well as a high coefficient of determination (R²). Similarly, the predicted and observed values displayed no significant (p > 0.05) differences. In addition, our enzyme characterization study revealed that Penicillium candidum (PCA 1/TT031) produced a slight neutral protease with a molecular weight between 100 and 140 kDa. The optimal activity of the purified enzyme occurred at a pH of 6.0 and at a temperature of 50 °C. The stability between different pH and temperature ranges along with the effect of chemical metal ions and inhibitors were also studied. Our results reveal that the purified enzyme could be used in the dairy industry such as in accelerated cheese ripening.
    Matched MeSH terms: Penicillium/enzymology*
  5. Ong SM, Voo LY, Lai NS, Stark MJ, Ho CC
    J Appl Microbiol, 2007 Mar;102(3):680-92.
    PMID: 17309617
    To identify novel microbial inhibitors of protein phosphatase 1 (PP1).
    Matched MeSH terms: Penicillium/enzymology
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