Esterification activity and stability of Talaromyces thermophilus lipase immobilized onto chitosan

Romdhane, Ines Belhaj-Ben; Romdhane, Zamen Ben; Gargouri, Ali; Belghith, Hafedh

doi:10.1016/j.molcatb.2010.11.010

Cited by 52 publications

(22 citation statements)

References 53 publications

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“…TTLI [15] TTLII (this study) Activity yield (%) 76.0 ± 3 32.0 ± 3 Activity (U/g carrier) 433 ± 16 91.2 ± 8 Immobilization yield (%) 91.0 ± 4 95.0 ± 3 Immobilized proteins (%) 70.0 ± 5 65.0 ± 6 the efficiency of the immobilized enzyme. We therefore can say that the interaction between the pre-activated carrier and the glycan favor a more correct orientation of the protein making it accessible to substrates.…”

Section: Enzymatic Formsmentioning

confidence: 79%

“…The two purified TTL forms were immobilized onto chitosane pre-activated with glutaraldehyde according to a previously described procedure [15].…”

Section: Covalent Immobilization Of the Two Ttl Formsmentioning

confidence: 99%

“…Our previous results have shown that Talaromyces thermophilus produces only one form of a detergent-stable alkaline lipase, termed as TTL, which was purified to homogeneity characterized and immobilized [14,15]. The N-terminal sequence analysis of the purified TTL indicated that is the product of the previously cloned gene product which encodes a protein of 269 Aa with an estimated molecular mass of 30 kDa [16].…”

Section: Introductionmentioning

confidence: 99%

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Purification, physico-chemical and kinetic properties of the deglycosylated Talaromyces thermophilus lipase

Romdhane

Fendri

Frikha

et al. 2012

International Journal of Biological Macromolecules

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Section: Enzymatic Formsmentioning

confidence: 79%

“…The two purified TTL forms were immobilized onto chitosane pre-activated with glutaraldehyde according to a previously described procedure [15].…”

Section: Covalent Immobilization Of the Two Ttl Formsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Purification, physico-chemical and kinetic properties of the deglycosylated Talaromyces thermophilus lipase

Romdhane

Fendri

Frikha

et al. 2012

International Journal of Biological Macromolecules

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“…capacidade de reuso por até 10 ciclos, com atividade residual entre 40% e 80% (Amorim et al, 2003;Romdhane et al, 2011;Ye et al, 2005). Comparado à enzima livre, o resultado foi ainda mais expressivo, visto que a lipase livre apresentou uma redução de 74,3% na atividade em apenas uma semana de armazenamento nas mesmas condições.…”

Section: Estabilidade Durante O Armazenamentounclassified

Imobilização de lipase em pectina extraída de frutos de lobeira (Solanum lycocarpum St. Hil.)

Filho

Torralbo

Di-Medeiros

et al. 2012

Biochem. Biotechnol. Rep.

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In this study, pectin extracted from the lobeira fruit (Solanum lycocarpum St. Hil) was used as support for lipase immobilization. The lobeira fruits were dried and the flour was used for pectin extraction. A 2 3 factorial design was used for the extraction process, with temperature, pH and extraction time as independent variables. Immobilization was performed by adsorption and covalent bonding using sodium periodate (PEC -P) or glutaraldehyde (PEC -G) as support activators. The results indicated that covalent bonding PEC -P was efficient in immobilizing the enzyme. The immobilization by adsorption and covalent bonding PEC -G did not provide storage stability. The stability tests results for the storage of the lipase-PEC-P system demonstrated that this system maintained 85,4% of enzyme activity after eleven weeks of storage. These results enable the use of pectin extracted from the Solanum lycocarpum (St. Hil.) fruit as a promising support for the immobilization of enzymes. RESUMONeste trabalho, pectina extraída de frutos de lobeira (Solanum lycocarpum St. Hil) foi utilizada como suporte para a imobilização de lipase. Os frutos de lobeira foram secos e a farinha utilizada para a extração da pectina. Para o processo de extração foi utilizado um planejamento fatorial 2 3 com temperatura, pH e tempo como variáveis independentes. A imobilização foi realizada por adsorção e por ligação covalente utilizando periodato de sódio (PEC-P) ou glutaraldeído (PEC-G) como ativadores do suporte. Os resultados indicaram que a ativação por PEC-P foi eficiente para a imobilização da enzima. A imobilização por adsorção e por ligação covalente para o suporte PEC-G não apresentaram estabilidade ao armazenamento. Os resultados para os testes de estabilidade ao armazenamento do sistema lipase-PEC-P demonstraram que este sistema manteve 85,4% da atividade enzimática após onze semanas de estocagem. Estes resultados habilitam a utilização da pectina extraída de lobeira como um suporte promissor para a imobilização de enzimas.Palavras-chave: pectina, imobilização, Solanum lycocarpum, lipase.

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“…The alkali and thermostable lipase from Talaromyces thermophilus performed remarkably in different conditions, endowing itself great potential in biodiesel production [8], paper making, and detergent ingredient [9]. Whereas, low productivity of this fungus held back its further applications.…”

Section: Introductionmentioning

confidence: 99%

Heterologous Expression of an Alkali and Thermotolerant Lipase from Talaromyces thermophilus in Trichoderma reesei

Zhang

Xia

2015

Appl Biochem Biotechnol

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To heterologously express a Talaromyces thermophilus lipase gene in Trichoderma reesei, an efficient binary vector pChph-pCBH1sigpro-ttl which includes a newly designed cbh1 promoter and hygromycin-resistant marker was constructed. This plasmid was then transformed into T. reesei via improved Agrobacterium EHA 105-mediated transformation. After modification of co-culture conditions and enzymolysis treatment of conidia, 258 transformants were produced. A two-step screening method based on antibiotic resistance and capacity to utilize lactose and tributyrin was introduced to further select promising candidates, which would be additionally verified by PCR analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and lipase activity assay. Lipase production was carried out in shaking flasks, and the activity reached 241 IU/mL (7415.4 IU/mg) after 84-h fermentation. It was found that this lipase performed high alkali and thermostable tolerance with the optimal pH 9.5 and temperature 60 °C, and it could retain more than 70 % activity after being disposed in pH 11 or 70 °C for 1 h. This study herein would benefit the genetic engineering of T. reesei and the industrial application of this important fungal lipase.

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Esterification activity and stability of Talaromyces thermophilus lipase immobilized onto chitosan

Cited by 52 publications

References 53 publications

Purification, physico-chemical and kinetic properties of the deglycosylated Talaromyces thermophilus lipase

Purification, physico-chemical and kinetic properties of the deglycosylated Talaromyces thermophilus lipase

Imobilização de lipase em pectina extraída de frutos de lobeira (Solanum lycocarpum St. Hil.)

Heterologous Expression of an Alkali and Thermotolerant Lipase from Talaromyces thermophilus in Trichoderma reesei

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