Cold active pectinases: Advancing the food industry to the next generation

Applied Biochemistry and Biotechnology

Volumn 172, Issue 5, 2014, Pages 2324-2337

  Adapa, Vijayanand ^a   Ramya, L N ^a   Pulicherla, K K ^b   Rao, K R S Sambasiva ^a  

^a ACHARYA NAGARJUNA UNIVERSITY   (India)

^b VIT UNIVERSITY   (India)

Author keywords

Cold active pectinase; Food processing; Pectin; Pectin lyases; Psychrophiles

Indexed keywords

MICROORGANISMS;

COLD-ADAPTED MICROORGANISMS; LOW TEMPERATURE PROCESSING; PECTIN; PECTIN LYASES; PECTINASES; PSYCHROPHILES; TEMPERATURE DEPENDENT; THERMOPHILIC MICROORGANISMS;

FOOD PROCESSING;

ASPERGILLUS NIGER; BACILLUS SUBTILIS; CARBOHYDRATE SEQUENCE; COLD CLIMATE; COLD TEMPERATURE; ERWINIA; FOOD HANDLING; HUMANS; ICE COVER; ISOENZYMES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PECTINS; POLYGALACTURONASE;

EID: 84899413364     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-013-0685-1     Document Type: Article

References (67)

1. Cabeza, M. S., Fanny, L. B., Ernesto, M. P., Flavia, L., Baigorí, M. D., & Morata, V. I. (2011). Selection of psychrotolerant cold-active pectinases for biotechnological process at low temperature. Food Technology and Biotechnology, 49(2), 187-195.
2. Dosanjh, N. S., & Hoondal, G. S. (1996). Production of constitutive, thermostable, hyperactive exopectinases form Bacillus GK-8. Biotechnology Letters, 18(12), 1435-1438.
3. Pedrolli, D. B., Monteiro, A. C., Gomes, E., & Carmona, E. C. (2009). Pectin and pectinases: production, characterization and industrial application of microbial pectinolytic enzymes. Open Biotechnology Journal, 3, 9-18.
4. Semenova, M. V., Sinitsyna, O. A., Morozova, V. V., Fedorova, E. A., Gusakov, A. V., Okunev, O. N., et al. (2006). Use of a prepration from fungal pectin lyase in the food industry. Applied Biochemistry and Microbiology, 42(6), 598-602.
5. Truong, L. V., Tuyen, H., Helmke, E., Binh, L. T., & Schweder, T. (2001). Cloning of two pectatelyase genes from the marine Antarctic bacterium Pseudoalteromonas haloplanktis strain ANT/505 and characterization of the enzymes. Extremophiles, 5(1), 35-44.
6. Pulicherla, K. K., Mrinimoy Ghosh, Suresh Kumar, P., & Sambasiva Rao, K. R. S. (2011). Psychrozymes - the next generation industrial enzymes. Journal of Marine Science: Research and Development, 1, 1.
7. Madden D. (2000). Enzymes in fruit juice production, In A Jam and out of juice (pp. 1-10), Version 1. http://www.ncbe.reading.ac.uk.
8. Harholt, J., Suttangkakul, A., & Scheller, H. V. (2010). Biosynthesis of pectin. Plant Physiology, 153, 384-395.
9. Caffall, K. H., & Mohnen, D. (2009). The structure, function, and biosynthesis of plant cell wall pectic polysaccharides. Carbohydrate Research, 344, 1879-1900.
10. Kashyap, D. R., Vohra, P. K., Chopra, S., & Tewari, R. (2001). Applications of pectinases in the commercial sector: a review. Bioresource Technology, 77, 215-227.
11. Prathyusha, K., & Suneetha, V. (2011). Bacterial pectinases and their potent biotechnological application in fruit processing/juice production industry: a review. Journal of Phytology, 3(6), 16-19.
12. Blanco, P., Sieiro, C., & Villa, T. G. (2009). Production of pectic enzymes in yeasts. FEMS Microbiology Letters, 175, 1-9.
13. Alkorta, I., Garbisu, C., Llama, M. J., & Serra, J. L. (1998). Industrial applications of pectic enzymes: a review. Process Biochemistry, 33, 21-28.
14. Whitaker, J. R. (1990). Microbial pectolytic enzymes, In W. M. Fogerty and G. T. kelly (Eds.), Microbial enzymes and biotechnology (pp. 133-176, 2nd edition.
15. Jayani, R. S., Saxena, S., & Gupta, R. (2005). Microbial pectinolytic enzymes: a review. Process Biochemistry, 40, 2931-2944.
16. Margesin, R., Neuner, G., & Storey, K. B. (2007). Cold-loving microbes, plants and animals - fundamental and applied aspects. Naturwissenschaften, 94, 77-99.
17. Gummadi, S. N., & Sunil Kumar, D. (2005). Microbial pectic transeliminases. Biotechnology Letters, 27, 451-458.
18. Waheeda, M. A., Jekayinfab, S. O., Ojediranb, J. O., & Imeokpariaa, O. E. (2008). Energetic analysis of fruit juice processing operations in Nigeria. Energy, 33, 35-45.
19. Vlugt-Bergman, C. J. B., Meeuwsen, P. J. A., Voragen, A. G. J., & Ooyen, A. J. J. (2000). Endo-Xylogalacturonan hydrolase, a novel pectinolytic enzyme. Applied and Environmental Microbiology, 66(1), 36-41.
20. Zandleven, J., Beldman, G., Bosveld, M., Benen, J., & Voragen, A. (2005). Mode of action of xylogalacturonan hydrolase towards xylogalacturonan and xylogalacturonan oligosaccharides. Biochemistry Journal, 387, 719-725.
21. Alimardani-Theuil, P., Gainvors-Claise, A., & Duchiron, F. (2011). Yeasts: an attractive source of pectinases - from gene expression to potential applications: a review. Process Biochemistry, 46, 1525-1537.
22. Hoondal, G. S., Tiwari, R. P., Tewari, R., Dahiya, N., & Beg, Q. K. (2002).Microbial alkaline pectinases and their industrial applications: a review. Applied Microbiology and Biotechnology, 59, 409-418.
23. Sakai, T., Sakamoto, T., Hallaert, J., Vandamme, E. J. (1993). Pectin, pectinase, and protopectinase: production, properties, and applications. Advances in Applied Microbiology (Vol. 39, pp. 213-294). London: Academic Press.
24. Lang, C., & Dornenburg, H. (2000). Perspectives in the biological function and the technological application of polygalacturonases. Applied Microbiology and Biotechnology, 53, 366-375.
25. Yoder, M. D., Keen, N. T., & Jurnak, F. (1993). New domain motif: the structure of pectatelyase C, a secreted plant virulence factor. Science, 260(5113), 1503-1507.
26. Thomas, L. M., Doan, C. N., Oliver, R. L., & Yoder, M. D. (2002). Structure of pectatelyase A: comparison to other isoforms. Acta Crystallographica Section D, 58, 1008-1015.
27. Lietzke, S. E., Keen, N. T., Yoder, M. D., & Jurnak, F. (1994). The three-dimensional structure of pectate lyase E, a plant virulence factor from Erwinia chrysanthemi. Plant Physiology, 106, 849-862.
28. Jenkins, J., Mayans, O., Smith, D., Worboys, K., & Pickersgill, R.W. (2001). Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site. Journal of Molecular Biology, 305, 951-960.
29. Mayans, O., Scott, M., Connerton, I., Gravesen, T., Benen, J., Visser, J., et al. (1997). Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate binding clefts of pectin and pectatelyases. Structure, 5, 677-689.
30. Pickersgill, R., Jenkins, J., Harris, G., Nasser, W., & Robert-Baudouy, J. (1994). The structure of Bacillus subtilis pectatelyase in complex with calcium. Nature Structural Biology, 1, 717-723.
31. Akita, M., Suzuki, A., Kobayashi, T., Ito, S., & Yamane, T. (2000). Crystallization and preliminary X-Ray analysis of high-alkaline pectate lyase. Acta Crystallographica Section D, 56, 749-750.
32. Vitali, J., Schick, B., Kester, H. C. M., Visser, J., & Jurnak, F. (1998). The three dimensional structure of Aspergillus niger pectin lyase B at 1.7-a resolution. Plant Physiology, 116, 69-80.
33. Pickersgill, R., Smith, D., Worboys, K., & Jenkins, J. (1998). Crystal structure of polygalacturonase from Erwinia carotovora ssp. carotovora. Journal of Biological Chemistry, 273, 24660-24664.
34. Van Pouderoyen, G., Snijder, H. J., Benen, J. A., & Dijkstra, B. W. (2003). Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger. FEBS Letters, 554, 462-466.
35. Van Santen, Y., Benen, J. A. E., Schroter, K. H., Kalk, K. H., Armand, S., Visser, J., et al. (1999). 1.68 - A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis. Journal of Biological Chemistry, 274, 30474-30480.
36. Johansson, K., El-Ahmad, M., Friemann, R., Jornvall, H., Markovic, O., & Eklund, H. (2002). Crystal structure of plant pectin methylesterase. FEBS Letters, 51, 243-249.
37. Di Matteo, A., Giovane, A., Raiola, A., Camardella, L., Bonivento, D., De Lorenzo, G., et al. (2005). Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein. Plant Cell, 17, 849-858.
38. S. N. Gummadi, N. Manoj, D. Sunil Kumar. (2007). Structural and biochemical properties of pectinases. In: J. Polaina and A.P. MacCabe (Eds.), Industrial Enzymes, 99-115.
39. Yoder, M. D., Lietzke, S. E., & Jurnak, F. (1993). Structure, 1, 241-251.
40. Hadj-Taieb, N., Ayadi, M., Trigui, S., Bouabdollah, F., & Gargouri, A. (2002). Hyper production of pectinase activities by fully constitutive mutant (CT 1) of Penicillium occitanis. Enzyme and Microbial Technology, 30, 662-666.
41. Christensen, T. M., Nielsen, J. E., Kreiberg, J. D., Rasmussen, P., & Mikkelsen, J. D. (2002). Pectin methyl esterase from orange fruit: characterization and localization by in-situ hybridization and immunohistochemistry. Planta, 206, 493-503.
42. Visser, J., & Voragen, A. G. J. (Eds.). (1996). Pectins and pectinases. Amsterdam: Elsevier.
43. McNeil, M., Darvil, A. G., Fry, S. C., & Albersheim, P. (1984). Annual Review Beach, 53, 625-663.
44. Collmer, A., & Keen, N. T. (1986). The role of pectic enzymes in plant pathogenesis. Annual Review of Phytopathology, 24, 383-409.
45. Feller, G., & Gerday, C. (2003). Psychrophilic enzymes: hot topics in cold adaptation. Nature Reviews Microbiology, 1, 200-208.
46. Cummings, S. P., & Black, G. W. (1999). Polymer hydrolysis in a cold climate. Extremophiles, 3, 81-87.
47. Birgisson, H., Delgado, O., Arroyo, L. G., Hatti-Kaul, R., & Mattiasson, B. (2003). Cold-adapted yeasts as producers of cold-active polygalacturonases. Extremophiles, 7, 185-193.
48. Margesin, R., Fauster, V., & Fonteyne, P. A. (2005). Characterization of cold-active pectatelyases from psychrophilic Mrakia frigida. Letters in Applied Microbiology, 40, 453-459.
49. Naga Padma, P., Anuradha, K., & Reddy, G. (2011). Pectinolytic yeast isolates for cold-active polygalacturonase production. Innovative Food Science and Emerging Technologies, 12, 178-181.
50. Nakagawa, T., Nagaoka, T., Taniguchi, S., Miyaji, T., & Tomizuka, N. (2004). Isolation and characterization of psychrophilic yeasts producing cold-adapted pectinolytic enzymes. Letters in Applied Microbiology, 38, 383-387.
51. Merin, M. G., Mendoza, L. M., Farías, M. E., & Morita de Ambrosini, V. M. (2011). Isolation and selection of yeasts from wine grape ecosystem secreting cold-active pectinolytic activity. International Journal of Food Microbiology, 147, 144-148.
52. Nakagawa, T., Yamada, K., Miyaji, T., & Tomizuka, N. (2002). Cold active pectinolytic activity of psychrophilic-basidiomycetous yeast Cystofilobasidium capitatum strain PPY-1. Journal of Bioscience and Bioengineering, 94, 175-177.
53. Hazel, J. R., & Williams, E. E. (1990). The role of alterations in membrane lipid composition in enabling phsyciological adapatation to organisms to their physical environment. Progress in Lipid Research, 29, 167-227.
54. Clark, M. S., Clarke, A., Cockell, S. C., Convey, P., & Detrich, H. W. (2004). Antartic genomics. Comparative and Functional Genomics, 5, 230-238.
55. Chattopadhyay, M. K. (2002). Mechanism of bacterial adaptation to low temperature - a review. Journal of Biosciences, 31, 157-165.
56. Yamashita, Y., Nakamura, N., Omiya, K., Nishikawa, J., & Kawahara, H. (2002). Identification of an antifreeze lipoprotein from Morazella sp. of Antarctic origin. Bioscience, Biotechnology, and Biochemistry, 66, 239-247.
57. Hochachka, P. W., & Somero, G. N. (1984). Biochemical adaptations (pp. 355-449). Princeton University Press: Princeton.
58. Somero, G. N. (2004). Adaptation of enzymes to temperature: searching for basic "strategies". Comparative Biochemistry and Physiology. Part B, Biochemistry and Molecular Biology, 139, 321-333.
59. Methe, B. A., Nelson, K. E., Deming, J. W., Momen, B., Melamud, E., Zhang, X. J., et al. (2005). The psychrophilic lifestyle as revealed by the genome sequence of Colwelliapsychrerythraea 34H through genomic and proteomic analyses. Proceedings of the National Academy of Sciences of the United States of America, 102, 10913-10918.
60. Ganga, A., Piñaga, F., Querol, A., Vallés, S., & Ramón, D. (2001). Cell-wall degrading enzymes in the release of grape aroma precursors. Food Science and Technology International, 7, 83-87.
61. Zoecklein, B. W., Marcy, J. E., Williams, J. M., & Jasinsky, Y. (1997). Effect of native yeasts and selected strains of Saccharomyces cerevisiae on glycosyl, glucose potential, olatile terpenes and selected aglycones of white Riesling (Vitisvinifera) wines. Journal of Food Composition and Analysis, 10, 55-65.
62. Takasawa, T., Sagisaka, K., Yagi, K., Uchiyama, K., Aoki, A., Takaoka, K., et al. (1997). Polygalacturonase isolated from the culture of the psychrophilic fungus Sclerotinia borealis. Canadian Journal of Microbiology, 43(5), 417-424.
63. Anuradha, K., Naga Padma, P., Venkateshwar, S., & Reddy, G. (2010). Fungal isolates from natural pectic substrates for polygalacturonase and multienzyme production. Indian Journal of Microbiology, 50, 339-344.
64. Van Rensburg, P., & Pretorius, I. S. (2000). Enzymes in winemaking: harnessing natural catalysts for efficient biotransformations - a review. South African Journal for Enology and Viticulture, 21. Special Issue.
65. Pulicherla, K. K., Suresh Kumar, P., Manideep, K., Rekha, V. P. B., Mrinmoy Ghosh, & Sambasiva Rao, K. R. S. (2013). Statistical approach for the enhanced production of cold active β-galactosidase from Thalassospira frigidphilosprofundus: a novel marine psychrophile from deep waters of Bay of Bengal. Preparative Biochemistry and Biotechnology, 43(8), 766-780.
66. Mrinmoy Ghosh, Pulicherla, K. K., Rekha, V. P. B., & Sambasiva Rao, K. R. S. (2013). Optimization of process condition for lactose hydrolysis in paneer whey with cold adaptive β-Galactosidase from psychrophilic Thalassospira frigidphilosprofundus. International Journal of Dairy Technology, 6(2), 256-263.
67. Mrinmoy Ghosh, Pulicherla, K. K., Rekha, V. P. B., & Sambasiva Rao, K. R. S. (2012). Cold active β-galactosidase from Thalassospira sp. 3SC-21 to use in milk lactose hydrolysis: a novel source from deep waters of Bay-of-Bengal. World Journal of Microbiology and Biotechnology, 28(9), 2859-2869.