Recombinant Pichia pastoris expressing ${omega}$-transaminase (TA) was used as a whole-cell biocatalyst to kinetically resolve ${alpha}$-methylbenzylamine (MBA). To overcome product inhibition of ${omega}$-TA by acetophenone (deaminated product of ${alpha}$-MBA), the reaction condition of endogenous oxidoreductases, which can catalyze the reduction of acetophenone into non-inhibitory 1-phenyl-ethanol, was optimized. When the whole-cell reaction was carried out using recombintat P. pastoris in 100 mM Tris/HCl buffer (pH 9.0) containing 2.5% glucose and 1% methanol, 100 mM ${alpha}$-MBA was successfully resolved to (R)-${alpha}$-MBA (> 99% ee) at a conversion of 52.2%.