Centre for Biotechnology and Interdisciplinary Sciences, Institute for Technology Research and Innovation (ITRI), Deakin University, Geelong, Victoria 3217, Australia.
Int J Biol Macromol. 2011 Jan 1;48(1):58-62. doi: 10.1016/j.ijbiomac.2010.09.012.
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+ (1 mM), 4-hydroxymercuribenzoate (0.1 mM) and cyanamide (0.1 mM). The purified enzyme established hydrolysis of naringin extracted from kinnow peel and thus endorses its industrial applicability for producing rhamnose.
橘红果皮是柑橘加工业的主要副产物，富含糖苷化酚类物质，其处理已成为一个主要问题。该果皮富含柚皮苷，可用α-L-鼠李糖苷酶（EC 3.2.1.40）生产鼠李糖，该酶能催化从柚皮苷中裂解末端鼠李糖基，生成圣草酚和鼠李糖。在这项工作中，红外（IR）光谱法证实了从橘红果皮废物中提取的柚皮苷的分子特征。此外，使用固定化金属螯合亲和层析（IMAC）从大肠杆菌细胞中纯化的重组α-L-鼠李糖苷酶用于柚皮苷水解。纯化的酶被 Hg2+（1mM）、4-羟基汞苯甲酸（0.1mM）和氰胺（0.1mM）抑制。纯化酶对从橘红果皮中提取的柚皮苷进行了水解，从而证明其在生产鼠李糖方面具有工业适用性。
