Phytases from Enterobacter and Serratia species with desirable characteristics for food and feed applications

Kalsi, Harpreet Kaur; Singh, Rajveer; Dhaliwal, H. S.; Kumar, Vinod

doi:10.1007/s13205-016-0378-x

Cited by 39 publications

(47 citation statements)

References 52 publications

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“…Klebsiella sp. and as well from other bacterial species, was found to be strongly inhibited by Mg 2+ (Escobin-Mopera et al, 2012;Hong, Chu, & Chung, 2011;Kalsi, Singh, Dhaliwal, & Kumar, 2016;Zhang et al, 2011).…”

Section: Discussionmentioning

confidence: 94%

Phytase Production from a Novel Klebsiella sp. on Wheat Bran for Animal Feed Digestion

Akter¹,

Khan²,

Mian³

et al. 2018

Microb. Bioacts.

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Background. The present study was aimed to isolate phytase producing bacteria and optimize the physicochemical parameters of their phytase production. Materials and methods. Four bacterial isolates (Phs4, Phs5, Phs6, and Phs8), based on clear zone formation on phytase screening medium, were selected and tested for finding out the highest phytase producing strain. The production of phytase was then optimized and its biochemical properties were determined to judge the applicability of phytase as a digestive aid in animal feed. Results. The 4 bacterial isolates (Phs4, Phs5, Phs6 and Phs8) were identified by morphological, cultural, biochemical and molecular characterization as Burkholderia cepacia, Escherichia coli, Klebsiella pneumoniae and Klebsiella sp. respectively. Of these isolates, Phs8 (Klebsiella sp.) was found to produce maximum phytase in shake culture in a basal medium containing Na-phytate at 37 o C and pH 5.5 after 72 hours of incubation. The omission of Na-phytate from the medium almost completely abolished the phytase production capacity of the isolate and thus signified its important role as an inducer. Among the different complex carbon sources, viz., glucose, wheat bran, rice bran and chickpea, maximum phytase production (94 unit/ ml) was obtained with wheat bran under comparable cultivation conditions. The phytase works best at a temperature of 37 o C and pH of 4.0 with a wide temperature stability (more than 80% activity up to 80 o C) and wide pH stability (more than 80% activity within a range of pH 3-8). Although Zn 2+ , Co 2+ , and Fe 2+ slightly increased the phytase activity Cu 2+ and Mg 2+ strongly inhibited the enzyme. Conclusion. The present findings will be very useful for the development of a bioprocess of the enzyme for its large-scale production at the pilot and finally at the commercial level.

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Section: Discussionmentioning

confidence: 94%

Phytase Production from a Novel Klebsiella sp. on Wheat Bran for Animal Feed Digestion

Akter¹,

Khan²,

Mian³

et al. 2018

Microb. Bioacts.

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“…In earlier studies, known phytate degrading organisms that include aerobic bacteria, anaerobic bacteria and fungi were isolated from different environmental conditions but fungi as a source of the higher phytase activity and cheaper than the other sources. Survey of microorganisms for selection of potential phytase producers was the subject of study by several workers Kalsi et al 2016;Kumar et al 2014b;Kumar et al 2013;Kumar et al 2016;Mukesh et al 2004;Yoon et al 1996). Different workers used multiple sources for isolation of phytase positive isolates including different kinds of soils, animals, plants and geographical locations.…”

Section: +mentioning

confidence: 99%

“…For efficient industrial application, a phytase which has high production, good activity at 37 °C, high activity and stability at broad pH range and ability to tolerate the high temperature are desirable characteristics. Therefore, most of the research on phytase has been focused on isolation and characterization of novel phytase with desirable characteristics from different sources (Huang et al 2009;Kalsi et al 2016;Kumar et al 2013;Mullaney et al 2010). Penicillium oxalicum has been reported as a promising phytase producing fungi with reports on characterization, heterogeneous expression and engineering of phytase from this fungi are available (Lee et al 2007;Lee et al 2015;Zhao et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Production and characterization of a neutral phytase of Penicillium oxalicum EUFR-3 isolated from Himalayan region

et al. 2017

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Abstract. Kaur R, Saxena A, Sangwan P, Yadav AN, Kumar V, Dhaliwal HC. 2017. Production and characterization of a neutral phytase of Penicillium oxalicum EUFR-3 isolated from Himalayan region. Nusantara Bioscience 9: 68-76. Micronutrient bioavailability from cereals is poor to monogastric animals due to presence of phytate as a chelating agent in seeds and an exogenous application of phytases is required to overcome antinutritional effect of phytate. In the present investigation, 40 fungal isolates including Aspergillus, Penicillium, Trichoderma, Toliposporium, Cladosporium, Talaromyces etc. from different habitats were screened positive for phytase activity on specific media. On the basis of phytase production potential in solid state fermentation conditions, plant epiphytic fungi Penicillium oxalicum strain EUFR-3 has been observed with maximum phytase activity of 12.8 U/g. The biochemical properties i.e. activity and stability under optimum pH and temperature, and effect of modulators on phytase activity from this isolate were studied for its prospective application in human food. The P. oxalicum EUFR-3 phytase (PhyP-EUFR3) had maximum activity at pH 7.0 and temperature 40 °C. It was stable in pH range of 3-8 with more than 60 % activity throughout investigation. The thermostability of PhyP-EUFR3 was about 30 % residual activities after 10 min at 80 °C. Further purification, characterization and study of catalytic mechanism will be useful in better utilization of this phytase in human food for increased bioavailability of important metal ions.

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“…Fungos termofílicos são microrganismos que crescem em altas temperaturas, cujas enzimas extracelulares podem ser ativas e estáveis sob condições de temperaturas superiores às enzimas produzidas por fungos mesofílicos, mostrando estabilidade em temperaturas próximas de 70 a 80°C, fornecendo dessa forma, vantagens econômicas na aplicação industrial (SINGH, 2016;WANG et al, 2015).…”

Section: Pmsfunclassified

“…O crescente mercado da fitase, gerado pelas suas inúmeras e importantes aplicações, tem impulsionado a busca por uma boa fonte da enzima, que possa atender aos diversos processos industriais (HUSSIN et al, 2007) e para isso uma grande variedade de tecidos animais, vegetais e microrganismos vem sendo prospectados (QUAN, et al, 2001;YAO et al, 2011), objetivando isolar e caracterizar novas fitases de diferentes fontes (KALSI et al, 2016). GUIMARÃES, 2016).…”

Section: Fontes De Fitasesunclassified

Clonagem, expressão e caracterização de fitase do fungo termofílico >i<Myceliophthora thermophila>/i<

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Fitases são enzimas que hidrolisam o ácido fítico, substâncias orgânicas complexas amplamente encontradas na natureza, principalmente em cereais e leguminosas. Nesses alimentos vegetais, o fitato é a principal fonte de fósforo, correspondendo entre cinquenta a oitenta por cento do conteúdo de fósforo orgânico. Entretanto, o fósforo do fitato é muito pouco utilizado por humanos e outros animais monogástricos, como suínos e aves, devido à ausência ou insuficiência das enzimas que o degradam. Assim, rações contêm o fósforo orgânico do fitato e fósforo inorgânico adicionado, que é um mineral caro e não renovável. Em áreas de criação intensiva o excesso de fósforo é excretado no ambiente, causando problemas, tais como a eutrofização. Devido aos problemas ambientais e ao alto custo do fósforo inorgânico, a suplementação de enzimas, principalmente fitases, tem ganhado destaque, entre elas, as enzimas fúngicas, devido a sua estabilidade a diferentes temperaturas e pH. Além disso, técnicas de engenharia genética permitem a transferência de genes entre espécies, resultando em muitos benefícios, principalmente em relação ao aumento e melhoramento na produção de enzimas industriais. O objetivo deste trabalho foi realizar a clonagem, expressão heteróloga, purificação e caracterização bioquímica da enzima fitase (MtPhy) obtida a partir do fungo termofílico M. thermophila. O gene que codifica a enzima foi clonado no vetor pEXPYR e heterologamente expresso em A. nidulans. A proteína recombinante foi purificada e teve sua identidade confirmada por espectrometria de massas. Nas análises bioquímicas, apresentou pH ótimo de 5,0 e temperatura ótima de 60°C e manteve praticamente 100% de sua atividade a 50°C por 2 horas e pela análise de dicroísmo circular e ThermoFluor, apresentou desenovelamento de sua estrutura nas temperaturas de 63 e 67°C, respectivamente. Demonstrou atividade aumentada na presença de CaCl 2 e MgCl 2 e foi fortemente inibida por FeCl 3 , CuSO 3 e SDS. Sua atividade específica (954,8 U/mg) utilizando fitato de sódio foi bastante superior a de outras fitases descritas na literatura. Demonstrou-se efetiva na liberação do fósforo em rações e extremamente resistente às proteases, tripsina e pepsina, presentes no trato digestório de animais monogástricos, demonstrando dessa forma, seu elevado potencial para aplicação industrial. Palavras-chave: Fitases. Fungos termofílicos. Myceliophtora thermophila.

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Phytases from Enterobacter and Serratia species with desirable characteristics for food and feed applications

Cited by 39 publications

References 52 publications

Phytase Production from a Novel Klebsiella sp. on Wheat Bran for Animal Feed Digestion

Phytase Production from a Novel Klebsiella sp. on Wheat Bran for Animal Feed Digestion

Production and characterization of a neutral phytase of Penicillium oxalicum EUFR-3 isolated from Himalayan region

Clonagem, expressão e caracterização de fitase do fungo termofílico >i<Myceliophthora thermophila>/i<

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