5 research outputs found
Marine chitinolytic enzymes, a biotechnological treasure hidden in the ocean?
No full textChitinolytic enzymes are capable to catalyze the chitin hydrolysis. Due to their biomedical and biotechnological applications,
nowadays chitinolytic enzymes have attracted worldwide attention. Chitinolytic enzymes have provided numerous useful materials in many different industries, such as food, pharmaceutical, cosmetic, or biomedical industry. Marine enzymes are commonly employed in industry because they display better operational properties than animal, plant, or bacterial homologs. In this
mini-review, we want to describe marine chitinolytic enzymes as versatile enzymes in different biotechnological fields. In this
regard, interesting comments about their biological role, reaction mechanism, production, functional characterization, immobilization, and biotechnological application are shown in this work.Beygmoradi, Azadeh-4357f5bc-fbca-487c-bd3f-f974a9fc2a62-600Homaei, Ahmad-0cc8be4a-ecd4-4ddf-9da7-1c55d129d669-600Hemmati, Roohullah-234501a6-44ca-44cc-8237-20488fcb6269-600Santos-Moriano, Paloma-4ab69e5b-7dab-4c12-a5d6-a1a9493b4384-600Hormigo, Daniel-915adee9-292d-4836-8d92-b79ac158d173-600Fernández-Lucas, Jesús-454d03d3-2cec-45b1-a796-51012f85b786-60
¿Las enzimas quitinolíticas marinas, un tesoro biotecnológico escondido en el océano? (revisión)
No full textChitinolytic enzymes are capable to catalyze the chitin hydrolysis. Due to their biomedical and biotechnological applications, nowadays chitinolytic enzymes have attracted worldwide attention. Chitinolytic enzymes have provided numerous useful materials in many different industries, such as food, pharmaceutical, cosmetic, or biomedical industry. Marine enzymes are commonly employed in industry because they display better operational properties than animal, plant, or bacterial homologs. In this mini-review, we want to describe marine chitinolytic enzymes as versatile enzymes in different biotechnological fields. In this regard, interesting comments about their biological role, reaction mechanism, production, functional characterization, immobilization, and biotechnological application are shown in this work.Las enzimas quitinolíticas son capaces de catalizar la hidrólisis de la quitina. Debido a sus aplicaciones biomédicas y biotecnológicas, en la actualidad las enzimas quitinolíticas han atraído la atención mundial. Las enzimas quitinolíticas han proporcionado numerosos materiales útiles en muchas industrias diferentes, como la industria alimentaria, farmacéutica, cosmética o biomédica. Las enzimas marinas se emplean comúnmente en la industria porque muestran mejores propiedades operativas que los homólogos de animales, plantas o bacterias. En esta mini revisión, queremos describir las enzimas quitinolíticas marinas como enzimas versátiles en diferentes campos biotecnológicos. En este sentido, se muestran comentarios interesantes sobre su papel biológico, mecanismo de reacción, producción, caracterización funcional, inmovilización y aplicación biotecnológica en este trabajo.Beygmoradi, Azadeh-4357f5bc-fbca-487c-bd3f-f974a9fc2a62-0Homaei, Ahmad-0cc8be4a-ecd4-4ddf-9da7-1c55d129d669-0Hemmati, Roohullah-234501a6-44ca-44cc-8237-20488fcb6269-0Santos Moriano, Paloma-4ab69e5b-7dab-4c12-a5d6-a1a9493b4384-0Hormigo, Daniel-915adee9-292d-4836-8d92-b79ac158d173-0Fernández Lucas, Jesús-454d03d3-2cec-45b1-a796-51012f85b786-
Identification of a novel tailor-made chitinase from white shrimp Fenneropenaeus merguiensis
No full textFenneropenaeus merguiensis (commonly named banana shrimp) is one of the most important farmed crustacean worldwide species for the fisheries and aquaculture industry. Besides its nutritional value, it is a good source of chitinase, an enzyme with excellent biological and catalytic properties for many industrial applications. In the present study, a putative chitinase-encoding cDNA was synthesized from mRNA from F. merguiensis hepatopancreas tissue. Subsequently, the corresponding cDNA was cloned, sequenced and functionally expressed in Escherichia coli, and the recombinant F. merguiensis chitinase (rFmCHI) was purified by His-tag affinity chromatography. The bioinformatics analysis of aminoacid sequence of rFmCHI displayed a cannonical multidomain architecture in chitinases which belongs to glycoside hydrolase family 18 (GH18 chitinase). Biochemical characterization revealed rFmCHI as a monomeric enzyme of molecular weight 52 kDa with maximum activity at 40 °C and pH 6.0 Moreover, the recombinant enzyme is also stable up to 60 °C, and in the pH range 5.0-8.0. Steady-state kinetic studies for colloidal chitin revealed KM, Vmax and kcat values of 78.18 μM, 0.07261 μM. min−1 and 43.37 s−1, respectively. Overall, our results aim to demonstrate the potential of rFmCHI as suitable catalyst for bioconversion of chitin waste.Sin financiación5.999 Q1 JCR 20210.882 Q1 SJR 2021No data IDR 2021UE
Identification of a novel tailor-made chitinase from white shrimp fenneropenaeus merguiensis
No full textFenneropenaeus merguiensis (commonly named banana shrimp) is one of the most important farmed crustacean worldwide species for the fisheries and aquaculture industry. Besides its nutritional value, it is a good source of chitinase, an enzyme with excellent biological and catalytic properties for many industrial applications. In the present study, a putative chitinase-encoding cDNA was synthesized from mRNA from F. merguiensis hepatopancreas tissue. Subsequently, the corresponding cDNA was cloned, sequenced and functionally expressed in Escherichia coli, and the recombinant F. merguiensis chitinase (rFmCHI) was purified by His-tag affinity chromatography. The bioinformatics analysis of aminoacid sequence of rFmCHI displayed a cannonical multidomain architecture in chitinases which belongs to glycoside hydrolase family 18 (GH18 chitinase). Biochemical characterization revealed rFmCHI as a monomeric enzyme of molecular weight 52 kDa with maximum activity at 40 °C and pH 6.0 Moreover, the recombinant enzyme is also stable up to 60 °C, and in the pH range 5.0-8.0. Steady-state kinetic studies for colloidal chitin revealed KM, Vmax and kcat values of 78.18 μM, 0.07261 μM. min−1 and 43.37 s−1, respectively. Overall, our results aim to demonstrate the potential of rFmCHI as suitable catalyst for bioconversion of chitin waste.Beygmoradi, AzadehHomaei, Ahmad-will be generated-orcid-0000-0001-9909-4761-600Hemmati, RoohullahDel Arco, Jon-will be generated-orcid-0000-0003-4646-492X-600Fernández-Lucas, Jesús-will be generated-orcid-0000-0001-7045-8306-60
