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2014 | 16 | 3 | 74-79
Tytuł artykułu

Future Applications of Apricot (Prunus Armeniaca Kaisa) ß Galactosidase in Dairy Industry

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
The present study demonstrates the immobilization of β galactosidase from apricots (Prunus armeniaca kaisa) on an inexpensive concanavalin A layered cellulose-alginate hybrid gel. Immobilized β galactosidase retained 78% of the initial activity after crosslinking by glutaraldehyde. It exhibited greater fraction of activity at both acidic and basic pH, and showed broad spectrum temperature optimum as compared to free enzyme. Moreover, immobilized enzyme exhibited higher thermal stability at 60°C and retained 80% of the original enzyme activity in presence of 3% galactose. The crosslinked immobilized enzyme showed improved hydrolysis of lactose from milk and whey in batch processes at 50°C as well as in continuous reactors operated at fl ow rate of 20 mL/h and 30 mL/h even after one month. Moreover, crosslinked adsorbed β galactosidase retained 76% activity even after its sixth repeated use, thereby promoting its use for lactose hydrolysis in various dairy products even for longer durations.
Wydawca

Rocznik
Tom
16
Numer
3
Strony
74-79
Opis fizyczny
Daty
wydano
2014-09-01
online
2014-10-03
Twórcy
  • King Abdulaziz University, Center of Excellence in Genomic and Medicine Research, Jeddah-21589, Saudi Arabia, saansari@kau.edu.sa
  • Ibn Sina National College for Medical Studies, Department of Biochemistry, Jeddah-21418, Saudi Arabia
  • King Abdulaziz University, Center of Excellence in Genomic and Medicine Research, Jeddah-21589, Saudi Arabia
  • Universiti Kebangsaan Malaysia, School of Chemical Sciences and Food Technology, Faculty of Science and Technology, 43600 Bangi, Selangor Darul Ehsan, Malaysia
  • King Abdulaziz University, Center of Excellence in Genomic and Medicine Research, Jeddah-21589, Saudi Arabia
  • King Abdulaziz University, Center of Excellence in Genomic and Medicine Research, Jeddah-21589, Saudi Arabia
  • Universiti Kebangsaan Malaysia, School of Chemical Sciences and Food Technology, Faculty of Science and Technology, 43600 Bangi, Selangor Darul Ehsan, Malaysia
Bibliografia
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  • 4. Ansari, S.A., Satar, R., Chibber, S. & Khan, M.J. (2013). Enhanced stability of Kluyveromyces lactis β galactosidase immobilized on glutaraldehyde modified multiwalled carbon nanotubes. J. Mol. Cat. B Enz. 97, 258-263. DOI: http://dx.doi.org/10.1016/j.molcatb.2013.09.008.[Crossref]
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  • 16. Ansari, S.A. & Husain, Q. (2011). Bioaffinity based immobilization of almond (Amygdalus communis) b galactosidase on Con A-layered calcium alginate-cellulose beads: its application in lactose hydrolysis in batch and continuous mode. Iran. J. Biotechnol. 9, 290-301. DOI: 10.4236/ijb.2011.534032.[Crossref]
  • 17. Dwevedi, A., Kumar, A., Singh, D.P., Srivastava, O.N., & Kayastha, A.M. (2009). Lactose nano-probe optimized using response surface methodology. Biosensors and Bioelectronics 25, 784-790. DOI: 10.1016/j.bios.2009.08.029.[Crossref]
  • 18. Kishore, D. & Kayastha, A.M. (2012). Optimization of immobilization conditions for chick pea β-galactosidase (CpGAL) to alkylamine glass using response surface methodology and its applications in lactose hydrolysis. Food Chemistry 134, 1113-1122. DOI:10.1016/j.foodchem.2012.03.055.[Crossref]
  • 19. Kishore, D., Talat, M., Srivastava, O.N. & Kayastha, A.M. (2012). Immobilization of β-galactosidase onto functionalized graphene nano-sheets using response surface methodology and its analytical applications towards milk and whey lactose. Plos One 7, e40708. DOI: 10.1371/journal.pone.0040708.[Crossref]
  • 20. Gulzar, S. & Amin, S. (2012). Kinetic studies on β-galactosidase isolated from apricots (Prunus armeniaca kaisa). Amer. J. Plant Sc. 3, 636-645. DOI: 10.4236/ajps.2012.35077.[Crossref]
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  • 22. Zhang, S., Gao, S. & Gao, G. (2010). Immobilization of β galactosidase onto magnetic beads. Appl. Biochem. Biotechnol. 160, 1386-1393. DOI: 10.5539/ijc.v5n4p38.[WoS][Crossref]
  • 23. Elnashar, M.M.M. & Yassin, M.A. (2009). Lactose hydrolysis by β galactosidase covalently immobilized to thermally stable biopolymers. Appl. Biochem. Biotechnol. 159, 426-437. DOI: 10.1007/s12010-008-8453-3.[Crossref][WoS]
  • 24. Park, A. & Oh, D. (2010). Effects of galactose and glucose on the hydrolysis reaction of a thermostable β galactosidase from Caldicellulosiruptor saccharolyticus. Appl. Microb. Biotechnol. 85, 1427-1435. DOI: 10.1007/s00253-009-2165-7.[Crossref]
  • 25. Kaur, G., Panesar, PS., Bera, MB. & Kumar, H. (2009). Hydrolysis of whey lactose using CTAB-permeabilized yeast cells. Bioproc. Biosyst. Eng. 32, 63-67. DOI: 10.1007/s00449-008-0221-9.[WoS][Crossref]
  • 26. Mammarella, E.J. & Rubiolo, A.C. (2006). Predicting the packed-bed reactor performance with immobilized microbial lactase. Proc. Biochem. 41, 1627-1636. DOI: 10.1016/j. procbio.2006.03.009.[Crossref]
  • 27. Panesar, R., Panesar, P.S., Singh, R.S., Kennedy, J.F. & Bera, M.B. (2007). Production of lactose hydrolyzed milk using ethanol permeabilized yeast cells. Food Chem. 101, 786-790. DOI: 10.1016/j.foodchem.2006.02.064.[Crossref][WoS]
  • 28. Szczodrak, J. (2000). Hydrolysis of lactose in whey permeate by immobilized β galactosidase from Kluveromyces fragilis. J. Mol. Catal. B: Enzym. 10, 631-637. DOI: 10.1016/ S1381-1177(00)00187-9.[Crossref]
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.-psjd-doi-10_2478_pjct-2014-0054
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