Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads

Cavello, Ivana Alejandra; Contreras-Esquivel, Juan Carlos; Cavalitto, Sebastián Fernando

doi:10.1016/j.procbio.2014.04.016

Cited by 35 publications

(20 citation statements)

References 29 publications

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“…In addition, there is growing concern related to the potential adverse health effects caused by GA, since it has been shown to induce eye, skin and upper respiratory tract irritation, as well as headaches, nausea, fatigue and occupational asthma (Takigawa and Endo 2006). Hence, alternative nontoxic support-activating reagents are currently being investigated (Cavello et al 2014). Sodium tri-polyphosphate (STPP), a substance "generally recognized as safe," is a multivalent anion that can form cross-links by ionic interaction between its multivalent negatively charged molecules and the positively charged amino groups (-NH3 1 ) of chitosan in acid medium (Fernandes et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Catalytic and Operational Stability of Acidic Proteases from Monterey Sardine (Sardinops sagax caerulea) Immobilized on a Partially Deacetylated Chitin Support

Salazar-Leyva

Lizardi‐Mendoza

Ramírez‐Suárez

et al. 2016

Journal of Food Biochemistry

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Recovery of valuable compounds from by‐products generated from seafood processing represents an opportunity to produce value‐added products. Sardine acidic proteases were immobilized on partially deacetylated chitin through ionic linkages, using sodium tripolyphosphate as a support activating agent. Maximal enzyme activities of free and immobilized proteases were detected at pH 2, at which the immobilized form had higher stability than the free enzymes. Optimum temperatures for free and immobilized proteases were 40 and 50C, respectively, while thermal stability of immobilized proteases was greater than that of free proteases. Reusability studies showed that after a second catalytic cycle, the immobilized enzyme maintained about 40% of the initial activity. The immobilization process enhanced the long term storage stability of sardine proteases compared to free enzymes. Results suggest that the immobilized enzyme could be used as a biotechnological aid for food processing when low pH and temperature around 50C are needed. Practical Applications Fish waste constitutes a serious environmental problem due to high disposal costs. Besides, this waste is commonly discarded or used for low value processes. Therefore, this study proposes the immobilization of sardine (Sardinops sagax caerulea) acidic proteases from fish viscera waste, on a partially deacetylated chitin support extracted from shrimp (Penaeus spp.) head. This research suggests that seafood protease immobilization onto chitinous supports presents an opportunity to improve the stability of these enzymes and consequently enhance potential application of these valuable biocatalysts as biotechnological aid, mainly for food processing and other value added products.

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Section: Introductionmentioning

confidence: 99%

Catalytic and Operational Stability of Acidic Proteases from Monterey Sardine (Sardinops sagax caerulea) Immobilized on a Partially Deacetylated Chitin Support

Salazar-Leyva

Lizardi‐Mendoza

Ramírez‐Suárez

et al. 2016

Journal of Food Biochemistry

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“…However, findings regarding their toxicity and irritation have limited any further biomedical application. 20 Therefore, to prepare uniform magnetic chitosan spheres with high saturation magnetization and excellent morphology using a facile and environmentally friendly method would be an attractive work.…”

Section: Introductionmentioning

confidence: 99%

Uniform Superparamagnetic Fe<SUB>3</SUB>O<SUB>4</SUB>/CMCS Composite Nanospheres for Lysozyme Adsorption

Yang¹,

Lan²,

Liu³

et al. 2016

j nanosci nanotechnol

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In this study, uniform superparamagnetic Fe3O4/carboxymethyl chitosan composite nanospheres with high saturation magnetization were successfully synthesized via a modified inverse emulsion crosslinking approach, using genipin as a cross-linking agent. These nanospheres were then characterized, and their protein adsorption capacity was further investigated under various conditions. The implementation of a sonication treatment of a mixture containing Fe3O4 nanoparticles and carboxymethyl chitosan before the emulsion process significantly promoted the homogeneity of Fe3O4 nanoparticles in an aqueous phase system. The Fe3O4/carboxymethyl chitosan composite nanospheres were of uniform spherical structure, were approximately 230 nm in size, and possessed superparamagnetic characteristics with a mean saturation magnetization as high as 35 emu g(-1), corresponding to a magnetite content of 43%. Lysozyme was then employed as a model protein to investigate the effects of pH, incubation time and ion strength on the protein adsorption capacity of the as-synthesized composite nanospheres. The as-obtained composite nanospheres could serve as a promising candidate for fast and efficient protein adsorption.

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“…In order to improve the performance of lipase on CMNPs, many cross‐linkers have been available for enzyme immobilization. Cross‐linkers consist of two groups: (1) synthetic cross‐linkers, such as glutaraldehyde and its derivatives, polyethylenimines, glycerol diglycidyl ether, p ‐benzoquinone; and (2) natural cross‐linkers, such as pectin and genipin . Among these cross‐linkers, glutaraldehyde and genipin have often been investigated in the literature.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, genipin has been proved to be an excellent natural cross‐linker for proteins and chitosan due to its remarkable stability and biocompatibility. Therefore genipin has been used to immobilize several enzymes such as β‐glycosidase, glucoamylase, naringinase, keratinase, and lipases . However, to the best of our knowledge, there exist few reports on comparison of the catalytic properties of lipase immobilized on CMNPs using genipin and glutaraldehyde as cross‐linker.…”

Section: Introductionmentioning

confidence: 99%

“…Cross-linkers consist of two groups: (1) synthetic cross-linkers, such as glutaraldehyde and its derivatives, 14 -16 polyethylenimines, 17 glycerol diglycidyl ether, 18 p-benzoquinone; 19 and (2) natural cross-linkers, such as pectin 20 and genipin. 21 -23 Among these cross-linkers, glutaraldehyde and genipin have often been investigated in the literature. Genipin is first extracted from the fruits of Gardenia jasminoides and can be obtained by enzymatic hydrolysis of geniposide.…”

Section: Introductionmentioning

confidence: 99%

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Stability and catalytic properties of lipase immobilized on chitosan encapsulated magnetic nanoparticles cross-linked with genipin and glutaraldehyde

Liu

Zhou

Wang

et al. 2015

J. Chem. Technol. Biotechnol.

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BACKGROUND Among many cross‐linkers for enzyme immobilization, genipin (Gen) and glutaraldehyde (Glu) as cross‐linkers have been commonly investigated to improve the catalytic performance of enzyme immobilized on chitosan encapsulated magnetic nanoparticles (CMNPs). In this work, we compared the stability and catalytic properties of lipase Candida rugosa (CRL) immobilized on CMNPs cross‐linked with Gen and Glu, respectively. The CMNPs were first characterized by TEM, XRD and FT‐IR. Moreover, some crucial parameters affecting catalytic performances were optimized for Gen‐CMNPs‐CRL and Glu‐CMNPs‐CRL preparation. RESULTS The Gen‐CMNPs‐CRL showed maximum activity at pH 8.0 and 40°C, and retained more than 95% of its initial activity after 7 days storage at 25°C. After 5 cycles re‐usage, Gen‐CMNPs‐CRL still retained over 80% of its initial activity, while Glu‐CMNPs‐CRL retained only 26% of its initial activity. Kinetic studies confirmed that Gen‐CMNPs‐CRL and Glu‐CMNPs‐CRL presented higher substrate affinity characteristics (Km) than free CRL. FT‐IR analysis showed that the variance of β‐sheet element in the secondary structure of CRL might contribute to the stability and activity enhancement of Gen‐CMNPs‐CRL. CONCLUSIONS Gen‐CMNPs‐CRL showed higher pH, temperature, storage and operational stabilities than Glu‐CMNPs‐CRL. Thus, genepin is a better promising cross‐linker than glutaraldehyde for lipase immobilization on CMNPs. © 2015 Society of Chemical Industry

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Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads

Cited by 35 publications

References 29 publications

Catalytic and Operational Stability of Acidic Proteases from Monterey Sardine (Sardinops sagax caerulea) Immobilized on a Partially Deacetylated Chitin Support

Catalytic and Operational Stability of Acidic Proteases from Monterey Sardine (Sardinops sagax caerulea) Immobilized on a Partially Deacetylated Chitin Support

Uniform Superparamagnetic Fe<SUB>3</SUB>O<SUB>4</SUB>/CMCS Composite Nanospheres for Lysozyme Adsorption

Stability and catalytic properties of lipase immobilized on chitosan encapsulated magnetic nanoparticles cross-linked with genipin and glutaraldehyde

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