Production of low methoxyl pectin using immobilized pectinmethylesterase silica from acerola (Malpighia glabra L.)

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Journal of Chemical Technology and Biotechnology

J Chem Technol Biotechnol 81:706–709 (2006) DOI: 10.1002/jctb.1382

Production of low methoxyl pectin using immobilized pectinmethylesterase silica from acerola (Malpighia glabra L.) Sandra A de Assis,1,2,3 Bruno S Ferreira,2,4 Pedro Fernandes,2,4,5 Henrique C Trevisan,1 Joaquim MS Cabral2 and Olga MMF Oliveira1∗ de Qu´ımica, Departamento de Bioqu´ımica e Tecnologia Qu´ımica, UNESP, Rua Prof. Francisco Degni, s/n.◦ – C.P. 355-CEP 14801-970, Araraquara, SP-Brazil 2 Centro de Engenharia Biologica ´ ´ e Qu´ımica, Instituto Superior Tecnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal 3 Departamento de Saude, Universidade Estadual de Feira de Santana, UEFS, Br 116, Km 03, Campus Universitario, ´ Feira de Santana, ´ 44031460, BA-Brazil 4 BioTrend, R. Torcato Jorge 41 c/v 2675-807 Ramada, Portugal 5 Universidade Lusofona ´ de Humanidades e Tecnologias, Av. Campo Grande 376, 1749-024 Lisboa, Portugal 1 Instituto

Abstract: The aim of this work was to develop an efficient reactor for the production of low methoxyl pectin, using pectinmethylesterase (PME, EC 3.1.1.11) from acerola immobilized on silica. The immobilized enzyme was used in up to 50 successive bioconversion runs at 50 ◦ C with an efficiency loss of less than 20%. The fixed-bed reactor (6.0 × 1.5 cm) was prepared using PME immobilized in glutaraldehyde-activated silica operated at 50 ◦ C with an optimum flow rate of 10 mL h−1 . The bioconversion yield was shown to strongly depend on the nature of the enzymatic preparation. An efficiency of 44% was achieved when concentrated PME was used, compared with only 30% with purified PME, both after an 8-h run. The process described could provide the basis for the development of a commercial-scale process.  2006 Society of Chemical Industry

Keywords: pectinmethylesterase; acerola; reactor; purification; immobilization

INTRODUCTION The enzyme pectinmethylesterase (PME, EC 3.1.1. 11), which has been found in plants as well as in pathogenic fungi and bacteria, catalyses the hydrolysis of the methyl ester groups from pectin.1 After this treatment, pectin can be further hydrolysed through the action of polygalacturonase. Plant PME has been used in the preparation of low methoxyl pectin (LMpectin) and in the destabilization of cloud in fruit juices.2,3 The use of soluble enzymes presents several disadvantages for a continuous process.4 These include the impossibility of reusing the enzymes or the alteration of the organoleptic properties of the processed product. Such drawbacks can be mitigated or even avoided by enzyme immobilization for continuous processing of fruit juice.4 With the new trends in industrial application of PME, there is an enhanced interest in the immobilization of this enzyme on insoluble carriers.5

Pectolytic enzymes play a crucial role in foodprocessing industries, for example, in the production of fruit juices, soft drinks, and liquors.6 These enzymes are used in the maceration, liquefaction, and extraction of vegetable tissues.6 They also help to reduce the viscosity of fruit pulp, which improves the filtration and clarification of fruit juices and wood aging.6 Pectinases are among these increasingly-important enzymes of the commercial sector.7 Pectin is widely used as a texturizer, stabilizer, and emulsifier in a wide variety of fields, among them the food and feed industry.8 Depending on the degree of methoxylation, pectins are classified into (1) LM- (low methoxyl, with a 25–50% degree of methoxylation) and (2) HM- (high methoxyl, with a 50–80% degree of methoxylation) pectins. These pectins can form gels of two types with occasional intermediates, which are called acid or calcium gels, depending on whether they are formed from HM or LM-pectins, respectively.8 The gels obtained from LM-pectins are softer, more

∗ Correspondence to: Olga MMF Oliveira, Instituto de Qu´ımica, Departamento de Bioqu´ımica e Tecnologia Qu´ımica, UNESP, Rua Prof. Francisco Degni, s/n.◦ – C.P. 355-CEP 14801-970, Araraquara, SP-Brazil E-mail: [email protected] Contract/grant sponsor: FAPESP Contract/grant sponsor: CAPES Contract/grant sponsor: PROPP-UNESP (Received 30 March 2005; revised version received 11 May 2005; accepted 13 May 2005) Published online 8 March 2006

 2006 Society of Chemical Industry. J Chem Technol Biotechnol 0268–2575/2006/$30.00

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Production of low methoxyl pectin

easily spread and relatively independent of pH, when compared with HM-pectin gels. Briggs9 suggested that pectins with both low methoxyl content and low molecular weight (
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