The use of isopropyl alcohol as a solvating agent in carboxymethyl cellulose production from nata de coco for invertase immobilization

Date

10-2000

Degree

Bachelor of Science in Chemistry

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Veronica C. Sabularse

Abstract

PLANTILLA, GRACE J. University of the Philippines Los Banos. October 2000. The Use of Isopropyl Alcohol as a Solvating Agent in Carboxymethvl Cellulose Production from Nata de coco for Invertase Immobilization.

Adviser: Dr. Veronica C. Sabularse

Carboxymethyl cellulose (CMC) was synthesized by the pre-treatment of bacterial cellulose (nata de coco) in isopropyl alcohol, followed by treatment with NaOH and monochloroacetic acid. The resulting carboxymethyl nata (CMN) samples which had been soaked for three and five hours in isopropyl alcohol had significantly higher degree of substitution (D.S.) than those soaked for one hour. The samples which had been soaked for one, three, and five hours in isopropyl alcohol produced CMN with D.S. of 0.05, 0.27, and 0.38, respectively; the corresponding solubility of the CMN samples were 6.02%, 26.04%, and 38.35%. An increasing trend in D.S. and solubility with length of soaking was observed. The ratio (w/v) of nata de coco pulp to isopropyl alcohol had no significant effect on the D.S. and solubility of the CMN produced.

The CMN used for invertase immobilization was synthesized from nata de coco pre-treated by soaking in isopropyl alcohol for seven hours at a ratio of 1:2 for nata de coco pulp to isopropyl alcohol. The CMN formed had a D.S. of 0.45, an intrinsic viscosity of 3.03 cps, an average molecular weight of 67,000 daltons, and a degree of polymerization (D.P.) of 413.

The relative activity of the invertase in CMN-agar compared to the free enzyme was 82%. A decreasing trend in activity of immobilized enzymes was observed with successive washings. For invertase immobilized in agar alone, specific activities (U/mg protein) for the first, second, and third washing were 8.50, 7.74, and 7.32, respectively; the corresponding specific activities for invertase immobilized in CMN-agar were 8.71, 8.17, and 7.39. However, the activity of the enzyme immobilized in CMN-agar had higher specific activities than that in agar alone, indicating that the enzyme was retained better in the presence of CMN.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 2000 C4 P53

Document Type

Thesis

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