Influence of carbon source, pH, and temperature on the polygalacturonase activity of Kluyveromyces marxianus CCMB 322

Oliveira, Rodrigo de Queiroz; Valasques, Gildomar Lima; Uetanabaro, Ana Paula Trovatti; Koblitz, María Gabriela Bello; Góes-Neto, Aristóteles; Rosa, Carlos A.; Assis, Sandra Aparecida de

doi:10.1590/s0101-20612012005000087

Cited by 4 publications

(3 citation statements)

References 15 publications

(17 reference statements)

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“…For example, Kluyveromyces, Saccharomyces , and Candida synthesize PG (i.e., endopolygalacturonase), while PG and PE are the major enzymes secreted by Rhodotorula ( Alimardani-Theuil et al, 2011 ). Oliveira et al (2012) investigated the impact of various pectic feedstocks, temperature, pH, and glucose on the polygalacturonase biosynthesis by K. marxianus CCMB 322. The enzyme secreted in the culture filtrate of K. marxianus CCMB 322 was found to be partially constitutive, exhibiting optimal temperature and pH of 70°C and 7.36, respectively.…”

Section: Applications In Biotechnological Productsmentioning

confidence: 99%

Bioprospecting Kluyveromyces marxianus as a Robust Host for Industrial Biotechnology

Bilal

et al. 2022

Front. Bioeng. Biotechnol.

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Kluyveromyces marxianus is an emerging non-conventional food-grade yeast that is generally isolated from diverse habitats, like kefir grain, fermented dairy products, sugar industry sewage, plants, and sisal leaves. A unique set of beneficial traits, such as fastest growth, thermotolerance, and broad substrate spectrum (i.e., hemi-cellulose hydrolysates, xylose, l-arabinose, d-mannose, galactose, maltose, sugar syrup molasses, cellobiose, and dairy industry) makes this yeast a particularly attractive host for applications in a variety of food and biotechnology industries. In contrast to Saccharomyces cerevisiae, most of the K. marxianus strains are apparently Crabtree-negative or having aerobic-respiring characteristics, and unlikely to endure aerobic alcoholic fermentation. This is a desirable phenotype for the large-scale biosynthesis of products associated with biomass formation because the formation of ethanol as an undesirable byproduct can be evaded under aerobic conditions. Herein, we discuss the current insight into the potential applications of K. marxianus as a robust yeast cell factory to produce various industrially pertinent enzymes, bioethanol, cell proteins, probiotic, fructose, and fructo-oligosaccharides, and vaccines, with excellent natural features. Moreover, the biotechnological improvement and development of new biotechnological tools, particularly CRISPR–Cas9-assisted precise genome editing in K. marxianus are delineated. Lastly, the ongoing challenges, concluding remarks, and future prospects for expanding the scope of K. marxianus utilization in modern biotechnology, food, feed, and pharmaceutical industries are also thoroughly vetted. In conclusion, it is critical to apprehend knowledge gaps around genes, metabolic pathways, key enzymes, and regulation for gaining a complete insight into the mechanism for producing relevant metabolites by K. marxianus.

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Section: Applications In Biotechnological Productsmentioning

confidence: 99%

Bioprospecting Kluyveromyces marxianus as a Robust Host for Industrial Biotechnology

Bilal

et al. 2022

Front. Bioeng. Biotechnol.

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“…A atividade pectinase das enzimas livres e imobilizadas foi determinada por espectrofotometria a 540 nm usando o método do ácido dinitrosalicílico modificado (Oliveira et al, 2012). Para a reação enzimática, a pectina cítrica foi utilizada como substrato por 30 min.…”

Section: Análise Da Atividade Da Pectinaseunclassified

Parâmetros De Encapsulação De Pectinase Comercial Em Alginato De Cálcio E Seu Efeito Na Atividade Catalítica

Carvalho¹,

Cardoso²,

Koblitz³

et al. 2020

Avanços Em Ciência E Tecnologia De Alimentos - Volume 2

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“…The pectinase activity of the free and immobilized enzymes was determined by spectrophotometry at 540 nm using the modified dinitrosalicylic acid method (Dliveira et al, 2012). For the enzymatic reaction, citric pectin was used as the substrate for 30 min.…”

Section: Analysis Of Pectinase Activitymentioning

confidence: 99%

Study of the parameters used in the encapsulation of commercial pectinase in calcium alginate and its effect on its catalytic activity

et al. 2019

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Despite the high catalytic properties of pectinases, the utilization of free enzymes always presents some hindrances such as low stability, a difficulty for product recovery and the impossibility of continuous use. Enzyme encapsulation is one of the methods used to overcome these limitations; however, some kind of effect is expected to occur on its catalytic activity. The objective of this work was to study the parameters involved in the process of encapsulation of a commercial pectinase product in calcium alginate and the effect of this encapsulation on its catalytic activity. The effect of the parameters of sodium alginate, calcium chloride, enzyme concentration and reaction time on enzymatic activity and encapsulation yield were also evaluated. The effect of pH and temperature on the activity of the free and encapsulated enzyme was studied. The highest yield of immobilization was obtained with a concentration of enzyme solution of 4%. Free and encapsulated enzymes showed similar behavior regarding the catalytic activity. The encapsulated enzyme had a narrower pH range (pH 4.0) than the free enzyme (pH 3.0 to 5.0). Besides, the encapsulated enzyme showed an increase in the stability in the pH range between 7 and 8 and above 10 to 12.

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Influence of carbon source, pH, and temperature on the polygalacturonase activity of Kluyveromyces marxianus CCMB 322

Cited by 4 publications

References 15 publications

Bioprospecting Kluyveromyces marxianus as a Robust Host for Industrial Biotechnology

Bioprospecting Kluyveromyces marxianus as a Robust Host for Industrial Biotechnology

Parâmetros De Encapsulação De Pectinase Comercial Em Alginato De Cálcio E Seu Efeito Na Atividade Catalítica

Study of the parameters used in the encapsulation of commercial pectinase in calcium alginate and its effect on its catalytic activity

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