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April Journal-2009.p65 - Association of Biotechnology and Pharmacy

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Current Trends in <strong>Biotechnology</strong> <strong>and</strong> <strong>Pharmacy</strong><br />

Vol. 3 (2) 172-180, <strong>April</strong> 2009. ISSN 0973-8916<br />

Production <strong>of</strong> á-amylase from agricultural byproducts by<br />

Humicola lanuginosa in solid state fermentation<br />

Ravi Kant Singh* a , Shashi Kumar b , <strong>and</strong> Surendra Kumar b<br />

a<br />

Department <strong>of</strong> <strong>Biotechnology</strong>, IMS Engineering College, Ghaziabad, U.P. India<br />

b<br />

Chemical Engineering Department, Indian Institute <strong>of</strong> Technology Roorkee, Roorkee 247 667, Uttarakh<strong>and</strong>, India<br />

*For correspondence - rksingh.iitr@hotmail.com<br />

Abstract<br />

In this study α-amylase activity<br />

expression in Humicola lanuginosa was<br />

evaluated under different environmental<br />

conditions using solid state fermentation (SSF)<br />

on different agricultural byproducts. The solid<br />

supports for α-amylase production in SSF process<br />

were wheat bran, wheat straw, rye straw, <strong>and</strong><br />

corncob leaf. Wheat bran has been found to yield<br />

maximum production <strong>of</strong> á-amylase among these<br />

solid substrates. Effects <strong>of</strong> process variables,<br />

namely incubation time & temperature, initial<br />

moisture content, pH, supplementary carbon<br />

source, <strong>and</strong> inoculum level, on production <strong>of</strong> α -<br />

amylase have been studied, <strong>and</strong> accordingly<br />

optimum conditions have been determined. It has<br />

been found that the á-amylase production is the<br />

highest at 144 hr incubation period, 50ºC<br />

incubation temperature, 90% initial moisture<br />

contents, pH <strong>of</strong> 6 <strong>and</strong> 20% inoculum level. Soluble<br />

starch has been found the best supplementary<br />

carbon source.<br />

Key words: solid state fermentation, Humicola<br />

lanuginosa, agricultural byproducts, α–amylase,<br />

process optimization, solid support.<br />

Introduction<br />

Enzyme production is an emerging field<br />

<strong>of</strong> biotechnology. At industrial scale, most <strong>of</strong> the<br />

enzymes are manufactured by submerged<br />

fermentation (SmF) techniques. However, in the<br />

last decades, there has been an increasing trend<br />

towards the utilization <strong>of</strong> the solid state<br />

fermentation (SSF) technique to produce several<br />

enzymes from thermophilic microorganisms (1-<br />

8). Few important advantages <strong>of</strong> solid state<br />

fermentation (SSF) over the traditionally employed<br />

submerged fermentation (SmF) are higher yields<br />

in a shorter time period, better oxygen circulation,<br />

resemblance to natural habitats for filamentous<br />

fungi, less effects in downstream processing, <strong>and</strong><br />

low energy consumption (9).<br />

Amylases are a group <strong>of</strong> enzymes that<br />

have been found in several microorganisms like<br />

bacteria (1,2,10,11) <strong>and</strong> fungi (3,12). α-amylases<br />

can be derived from plants, animals <strong>and</strong> microbes<br />

but its production from microbial sources are cost<br />

effective <strong>and</strong> fulfill the industrial dem<strong>and</strong>s. The<br />

large number <strong>of</strong> α- amylases are available<br />

commercially <strong>and</strong> they have almost completely<br />

replaced chemical hydrolysis <strong>of</strong> starch (13).<br />

Amylases are useful in a broad range <strong>of</strong> industrial<br />

applications which include food, fermentation,<br />

textile <strong>and</strong> paper industries.<br />

Fungal α-amylases are produced by<br />

different fermentation techniques. Production <strong>of</strong><br />

these α-amylases has been investigated through<br />

submerged fermentation (SmF) <strong>and</strong> solid state<br />

Production <strong>of</strong> á-amylase

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