Melezitose degrading microorganisms from fermented bamboo shoots

This study is focused on the melezitose-degrading enzyme, originating from fermenting bamboo shoots, to produce α-glucosidase for the breakdown of melezitose into turanose and glucose. The enzyme was produced by growing the microorganisms, isolated from fermented bamboo shoots, in melezitose, and maltose. This in turn increased the total protein concentration of both extracellular and intracellular enzymes. The optimum temperature for the action of the enzyme is 32?C. It showed high catalytic activity for isomaltose-like sugars such as palatinose, and among the maltose-like sugars, it is specific to melezitose. The enzyme exhibits broad substrate specificity and is promiscuous. The enzyme followed Michaelis-Menten kinetics and the Km and Vmax values were calculated using the Lineweaver-Burk plot. However, it can also catalyze the cleavage of other glycosidic bonds such as α-(1,1), α-(1,2), α-(1,4), and α-(1,6) linkages of trehalose, sucrose, maltose, and raffinose, respectively. The M/S ratio was introduced to observe the kinetic pattern, and it is correlated with Vmax. Among the metal ions studied, the potassium (K ⁺), ferrous (Fe²⁺), sodium (Na⁺), and zinc (Zn ²⁺) ions positively influenced the enzyme activity and might act as cofactors. This melezitose degrading enzyme (α-glucosidase) was tested on (artificial) honeydew-contaminated cotton. Based on qualitative and quantitative examinations such as microscopic, UV test, Benedict's test, Elsner colorimetric test, High volume instrument (HVI), and viscometer test results, it has been verified that the enzyme reduces the stickiness of cotton. Thus, this enzyme finds textile applications, where it can be applied to sticky cotton before textile processing, and it shall cause reduction of stickiness.