Affiliation:
1. College of Forestry Shanxi Agricultural University Taigu Shanxi P. R. China
2. Biotechnology Research Institute Chinese Academy of Agricultural Sciences Beijing P. R. China
3. Lucile Packard Children's Hospital at Stanford Palo Alto CA USA
Abstract
Abstract
A pectin lyase gene pnlzj5b from Aspergillus niger ZJ5 was identified and overexpressed successfully in Pichia pastoris. Recombinant PNLZJ5B exhibited high activity towards citrus pectin (150 U ml−1). Through further codon optimization, the expression efficiency of PNLZJ5B in P. pastoris increased to 3·5-fold (532/150 U ml−1). PNLZJ5B was purified by ultrafiltration, anion exchange and gel chromatography. It showed optimal activity and good stability at 58°C and pH 4·5. PNLZJ5B activity improved with increasing degrees of methyl esterification of pectin. The Km and Vmax values were 0·81 mg ml−1 and 372·8 μmol min−1 mg−1, respectively. In addition, PNLZJ5B effectively decreased the viscosity of apple juice. Compared with commercial pectin lyase, PNLZJ5B obtained a higher juice volume. These favourable enzymatic properties of PNLZJ5B show potential utility in juice-processing applications and other food-related fields.
Funder
Central Public-interest Scientific Institution Basal Research Fund for Chinese Academy of Tropical Agricultural Sciences
National High Technology Research and Development Program of China
National Natural Science Foundation of China
Publisher
Oxford University Press (OUP)
Subject
Applied Microbiology and Biotechnology
Cited by
1 articles.
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