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Co-conjugation vis-a-vis individual conjugation of α-amylase and glucoamylase for hydrolysis of starch

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논문

Co-conjugation vis-a-vis individual conjugation of α-amylase and glucoamylase for hydrolysis of starch

학술지

Carbohydrate polymers

저자명

Jadhav, S.B.; Singhal, R.S.

초록

Two enzymes, &alpha;-amylase and glucoamylase have been individually and co-conjugated to pectin by covalent binding. Both the enzyme systems showed better thermal and pH stability over the free enzyme system with the complete retention of original activities. Mixture of individually conjugated enzymes showed lower inactivation rate constant with longer half life than the co-conjugated enzyme system. Individually conjugated enzymes showed an increase of 56.48kJ/mole and 38.22kJ/mole in activation energy for denaturation than the free enzymes and co-conjugated enzymes, respectively. K<SUB>m</SUB> as well as V<SUB>max</SUB> of individually and co-conjugated enzymes was found to be higher than the free enzymes. SDS-polyacrylamide gel electrophoresis confirmed the formation of conjugate and co-conjugate as evident by increased molecular weight. Both the enzyme systems were used for starch hydrolysis where individually conjugated enzymes showed highest release of glucose at 60<SUP>o</SUP>C and pH 5.0 as compared to free and co-conjugated enzyme.

발행연도

2013

발행기관

Applied Science Publishers ; Elsevier Science Ltd

ISSN

0144-8617

98

1

페이지

pp.1191-1197

주제어

Stability; Starch hydrolysis; Co-conjugate; Inactivation rate constant; Activation energy

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1 2023-12-11

논문; 2013-10-01

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