Molecular characterization and enzymatic hydrolysis of naringin extracted from kinnow peel waste

Munish Puri, Aneet Kaur, Wolfgang Schwarz, Satbir Singh, J. F. Kennedy

    Research output: Contribution to journalArticlepeer-review

    23 Citations (Scopus)

    Abstract

    Kinnow peel, a waste rich in glycosylated phenolic substances, is the principal by-product of the citrus fruit processing industry and its disposal is becoming a major problem. This peel is rich in naringin and may be used for rhamnose production by utilizing α-l-rhamnosidase (EC 3.2.1.40), an enzyme that catalyzes the cleavage of terminal rhamnosyl groups from naringin to yield prunin and rhamnose. In this work, infrared (IR) spectroscopy confirmed molecular characteristics of naringin extracted from kinnow peel waste. Further, recombinant α-l-rhamnosidase purified from Escherichia coli cells using immobilized metal-chelate affinity chromatography (IMAC) was used for naringin hydrolysis. The purified enzyme was inhibited by Hg2+ (1mM), 4-hydroxymercuribenzoate (0.1mM) and cyanamide (0.1mM). The purified enzyme established hydrolysis of naringin extracted from kinnow peel and thus endorses its industrial applicability for producing rhamnose.

    Original languageEnglish
    Pages (from-to)58-62
    Number of pages5
    JournalINTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
    Volume48
    Issue number1
    DOIs
    Publication statusPublished - 1 Jan 2011

    Keywords

    • Citrus
    • IMAC
    • Infrared spectroscopy
    • Inhibitor
    • Naringin
    • Recombinant rhamnosidase

    Fingerprint Dive into the research topics of 'Molecular characterization and enzymatic hydrolysis of naringin extracted from kinnow peel waste'. Together they form a unique fingerprint.

    Cite this